MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins. Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins. FEBS Lett. (0014-5793) 2012 imex curation Mishra S., Stein RA., McHaourab HS. suggested by lperfetto Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Mishra S., Stein RA., McHaourab HS. suggested by lperfetto FEBS Lett. (0014-5793) 2012 Only protein-protein interactions imex curation Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins. Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins. FEBS Lett. (0014-5793) 2012 imex curation Mishra S., Stein RA., McHaourab HS. suggested by lperfetto Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Mishra S., Stein RA., McHaourab HS. suggested by lperfetto FEBS Lett. (0014-5793) 2012 Only protein-protein interactions imex curation cryab_mouse Alpha-crystallin B chain Cryab Crya2 Alpha(B)-crystallin P23 protein protein mouse Mus musculus Mouse MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVAAAPKK DIP protein P23927 original sequence version: 94 46702976C008EFD3 cryaa_rat Alpha-crystallin A chain Cryaa Crya1 protein protein rat Rattus norvegicus (Rat) Rat MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMWFVMHQPHAGNPKNNPGKVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS mint D0C0E0DFA82D551C crgd_human Gamma-crystallin D Gamma-crystallin 4 CRYGD CRYG4 Gamma-D-crystallin protein protein human Homo sapiens Human MGKITLYEDRGFQGRHYECSSDHPNLQPYLSRCNSARVDSGCWMLYEQPNYSGLQYFLRRGDYADHQQWMGLSDSVRSCRLIPHSGSHRIRLYEREDYRGQMIEFTEDCSCLQDRFRFNEIHSLNVLEGSWVLYELSNYRGRQYLLMPGDYRRYQDWGATNARVGSLRRVIDFS DIP protein P07320 original sequence version: 98 mint homomint 437EC83FD79F12E4 cryab-crygd 1 gammaD crystallin 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P07320:p.Ile4Phe mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I F Tue Jul 12 10:52:00 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 19:14:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile4phe' Tue Jun 30 15:43:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile4Phe' P07320:p.Val76Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V D Tue Jul 12 10:11:23 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 14:31:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val76asp' Tue Jun 30 15:58:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val76Asp' alphaB Crystallin 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P23927:p.Ser45Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S D Tue Jul 12 10:11:21 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 19:07:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser45asp' Tue Jun 30 18:59:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser45Asp' P23927:p.Ser19Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S D Tue Jul 12 10:51:58 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 14:47:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser19asp' Tue Jun 30 18:36:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser19Asp' P23927:p.Ser59Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S D Tue Jul 12 10:11:29 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 14:48:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser59asp' Tue Jun 30 17:28:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser59Asp' direct interaction direct interaction homomint mint f5b f5c In agreement with the conclusion of Figure 4, SEC analysis indicates that alphaB-D3 has the highest affinity to the gammaD-crystallin mutants showing detectable binding even for the two single mutants (Figure 5B). Figure 5A shows that incubation of alphaA-crystallin with WT gammaD-crystallin or the single mutants I4F (data not shown) and V76D does not result in detectable binding. In contrast, incubation with the double I4F/V76D leads to the concomitant reduction in the alpha-crystallin peak intensity (both absorbance and fluorescence) and appearance of a fluorescence peak migrating with a retention time similar to the chaperone. This indicates the formation of a stable complex between the two proteins. cryaa-crygd 1 alphaA Crystallin 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified gammaD Crystallin 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P07320:p.Val76Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V D Tue Jul 12 10:17:03 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 15:49:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val76asp' Tue Jun 30 15:54:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val76Asp' P07320:p.Ile4Phe mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I F Tue Jul 12 10:17:07 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 15:43:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile4phe' Tue Jun 30 15:41:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile4Phe' direct interaction direct interaction f5a mint Figure 5A shows that incubation of alphaA-crystallin with WT gammaD-crystallin or the single mutants I4F (data not shown) and V76D does not result in detectable binding. In contrast, incubation with the double I4F/V76D leads to the concomitant reduction in the alpha-crystallin peak intensity (both absorbance and fluorescence) and appearance of a fluorescence peak migrating with a retention time similar to the chaperone. This indicates the formation of a stable complex between the two proteins. cryaa-crygd-1 2 gammaD Crystallin 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P07320:p.Val76Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V D Tue Jul 12 10:54:46 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 16:54:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val76asp' Tue Jun 30 19:37:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val76Asp' P07320:p.Ile4Phe mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I F Tue Jul 12 10:16:35 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 15:07:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile4phe' Tue Jun 30 17:35:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile4Phe' alphaA Crystallin 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f4a mint Further destabilization of gammaD-crystallin native state by the combination of I4F and V76D is sufficient to promote stable binding to alphaA-crystallin. cryab-crygd-1 2 gammaD crystallin 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P07320:p.Val76Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V D Tue Jul 12 10:19:35 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 19:22:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val76asp' Tue Jun 30 19:31:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val76Asp' P07320:p.Ile4Phe mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I F Tue Jul 12 10:19:34 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 14:26:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile4phe' Tue Jun 30 16:49:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile4Phe' alphaB Crystallin 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P23927:p.Ser45Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S D Tue Jul 12 10:19:37 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 15:49:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser45asp' Tue Jun 30 20:17:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser45Asp' P23927:p.Ser59Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S D Tue Jul 12 10:19:36 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 14:38:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser59asp' Tue Jun 30 18:50:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser59Asp' P23927:p.Ser19Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S D Tue Jul 12 10:19:33 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 17:56:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser19asp' Tue Jun 30 18:52:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser19Asp' direct interaction direct interaction f4b homomint mint Neither alphaA-crystallin nor alphaB-crystallin chaperone binds WT gammaD-crystallin at detectable level; even at high concentrations and molar ratios (data not shown).While the double mutant did not effectively bind alphaB-crystallin, it formed stable complexes with its phosphorylation mimic (Figure 4B)