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 The Drosophila peptidoglycan-recognition protein LF interacts with peptidoglycan-recognition protein LC to downregulate the Imd pathway. The Drosophila peptidoglycan-recognition protein LF interacts with peptidoglycan-recognition protein LC to downregulate the Imd pathway. EMBO Rep. (1469-221X) 2011 imex curation Basbous N., Coste F., Leone P., Vincentelli R., Royet J., Kellenberger C., Roussel A. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Basbous N., Coste F., Leone P., Vincentelli R., Royet J., Kellenberger C., Roussel A. EMBO Rep. (1469-221X) 2011 Only protein-protein interactions imex curation pgplf_drome Peptidoglycan-recognition protein LF PGRP-LF PGRP-like protein CG4437 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MPKTVVVTHPGKPINNEKRFRFELLYFCVILLMVVGLAAGYFMWMMSFSTHSPNKGLHILDRSEWLGEPPSGKYPHLKLPVSNIIIHHTATEGCEQEDVCIYRMKTIQAFHMKSFGWVDIGYNFLVGGDGQIYVGRGWHIQGQHVNGYGAISVSIAFIGTFVNMEPPARQIEAAKRLMDEGVRLHRLQPDYHIYAHRQLSPTESPGQKLFELMQNWPRFTQDPTSLRLLSNETVKIVTRPYWLAQPPIVPLTPLKLPIESVRFVATNTPSCFTQAECTFRVRLLQNWHIESNGYKDINYNFVAAGDENIYEARGWDHSCEPPKDADELVVAFIGPSSSNKKIALELIKQGIKLGHISKNYSLIDDLEKS mint 01465701EE5DD289 pgplc_drome Peptidoglycan-recognition protein LC PGRP-LC ird7 Immune response deficient 7 protein PGRPLC CG4432 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MPFSNETEMSQCSNAKRRVNDPLTGPKNCSTSSTDSGVILNDNVAAFRPEKETKDRGTGEGQFQSKSEEKTESKRISVEHTVNITTENVGKTSSPAVSIRSTTISVVSIDDNAIDSSSIDSDSEAEAEDYTVQKLGHQVTYPPNSSHLRDLNQGLTVISRHVAPGEAAVPPPNPLEAGIVAKQILNGNLAVATPTSPAGGATQGIGSIALTNSTDVTFGDKHFYEGPVTIQQFLIDNRDKWKPGEGPAGGQDNPAFNGGPSTNGSAPGSKHEDPAQTPPICPFLPNTVGRKAVTVTVVFVTLTFLLGIVLATTTNLFGKTLNQSKIRDDDDYRQNIPINSTIDLDNIGGGLILRFVERQQWLAQPPQKEIPDLELPVGLVIALPTNSENCSTQAICVLRVRLLQTYDIESSQKCDIAYNFLIGGDGNVYVGRGWNKMGAHMNNINYDSQSLSFAYIGSFKTIQPSAKQLSVTRLLLERGVKLGKIAPSYRFTASSKLMPSVTDFKADALYASFANWTHWS 3215F8380857DFC1 pgrp_lc-pgrp_lf 1 PGRP-LF 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PGRP-LCx 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4 mint We demonstrate that, in the absence of TCT, LF displays the same weak affinity for LCx as LCa does for LCx. The same series of concentrations of LCa with a constant amount of TCT resulted in an increased response (approximately sevenfold). The affinity constant, Kd, of LCa LCx binding was 18.3±8.3 mM (95% confidence interval). When the same experiment was performed with LF in the presence of TCT, the responses were similar to those measured with LCa, with a calculated Kd of 17.6±6.1 mM (Fig 4). Injection of TCT alone or the Lys-type PGN-binding protein PGRPSA (20 mM), in the presence and absence of TCT, gave negligible responses (10 20 refractive units). In conclusion, SPR imaging studies confirm that TCT strongly enhances interactions with LCx, and show that LF interacts with LCx in a similar way to LCa, in the absence and presence of TCT. pgrp_lc-pgrp_lc 1 PGRP-LCa 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PGRP-LCx 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction f4b mint We demonstrate that, in the absence of TCT, LF displays the same weak affinity for LCx as LCa does for LCx. The same series of concentrations of LCa with a constant amount of TCT resulted in an increased response (approximately sevenfold). The affinity constant, Kd, of LCa LCx binding was 18.3±8.3 mM (95% confidence interval). When the same experiment was performed with LF in the presence of TCT, the responses were similar to those measured with LCa, with a calculated Kd of 17.6±6.1 mM (Fig 4). Injection of TCT alone or the Lys-type PGN-binding protein PGRPSA (20 mM), in the presence and absence of TCT, gave negligible responses (10 20 refractive units). In conclusion, SPR imaging studies confirm that TCT strongly enhances interactions with LCx, and show that LF interacts with LCx in a similar way to LCa, in the absence and presence of TCT.