DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ di-1997-1 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Di Marco S., Priestle JP. DIP original experiment: DIP-263251X Structure (London, England : 1993) 1997 IMEx Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system. Di Marco S., Priestle JP. Only protein-protein interactions imex curation tryp_pig Trypsin protein protein pig Sus scrofa (Pig) Pig FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN mint ldti_hirme Leech-derived tryptase inhibitor C protein protein medicinal leech Hirudo medicinalis KKVCACPKILKPVCGSDGRTYANSCIARCNGVSIKSEGSCPTGILN mint Acts as an inhibitor of human tryptase, trypsin and chymotrypsin. Probably acts to block host defense mechanisms ldti_hirme-tryp_pig-1 3293364 N/A 3293365 unspecified role unspecified role unspecified role unspecified role yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast N/A 3293366 unspecified role unspecified role unspecified role unspecified role pig Sus scrofa (Pig) Pig direct interaction direct interaction false false false 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 http://mint.bio.uniroma2.it/mint frigerio-1992-1 Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Frigerio F., Coda A., Pugliese L., Lionetti C., Menegatti E., Amiconi G., Schnebli HP., Ascenzi P., Bolognesi M. J. Mol. Biol. (0022-2836) 1992 gros-1989-1 Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 A resolution and comparison of two crystal forms that differ in calcium content. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Gros P., Betzel C., Dauter Z., Wilson KS., Hol WG. J. Mol. Biol. (0022-2836) 1989 heinz-1991-1 Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Heinz DW., Priestle JP., Rahuel J., Wilson KS., Grütter MG. J. Mol. Biol. (0022-2836) 1991 dauter-1991-1 Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dauter Z., Betzel C., Genov N., Pipon N., Wilson KS. Acta Crystallogr., B (0108-7681) 1991 stubbs-1997-1 The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Stubbs MT., Morenweiser R., Stürzebecher J., Bauer M., Bode W., Huber R., Piechottka GP., Matschiner G., Sommerhoff CP., Fritz H., Auerswald EA. J. Biol. Chem. (0021-9258) 1997 bode-1987-1 The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bode W., Papamokos E., Musil D. Eur. J. Biochem. (0014-2956) 1987 reverter-2000-1 Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Reverter D., Fernández-Catalán C., Baumgartner R., Pfänder R., Huber R., Bode W., Vendrell J., Holak TA., Avilés FX. Nat. Struct. Biol. (1072-8368) 2000 cbpa2_human Carboxypeptidase A2 CPA2 protein protein human Homo sapiens Human MAMRLILFFGALFGHIYCLETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVRVPFVNVQAVKVFLESQGIAYSIMIEDVQVLLDKENEEMLFNRRRERSGNFNFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFLLPVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWDAGFGGPGASSNPCSDSYHGPSANSEVEVKSIVDFIKSHGKVKAFITLHSYSQLLMFPYGYKCTKLDDFDELSEVAQKAAQSLRSLHGTKYKVGPICSVIYQASGGSIDWSYDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHVRDHPY mint mcpi_hirme Metallocarboxypeptidase inhibitor Leech carboxypeptidase inhibitor protein protein medicinal leech Hirudo medicinalis MFLLVFLCCLHLVISSHTPDESFLCYQPDQVCCFICRGAAPLPSEGECNPHPTAPWCREGAVEWVPYSTGQCRTTCIPYVE mint Tightly binding, competitive inhibitor of different types of pancreatic-like carboxypeptidases icic_hirme Eglin C protein protein medicinal leech Hirudo medicinalis TEFGSELKSFPEVVGKTVDQAREYFTLHYPQYDVYFLPEGSPVTLDLRYNRVRVFYNPGTNVVNHVPHVG mint Inhibits both elastase and cathepsin G ctra_bovin Chymotrypsinogen A protein protein bovin Bos taurus (Bovine) Bovine CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN subt_bacam Subtilisin BPN' apr Subtilisin Novo Subtilisin DFE Alkaline protease protein protein bacam Bacillus amyloliquefaciens MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ subt_bacpu Subtilisin apr Alkaline mesentericopeptidase protein protein bacpu Bacillus pumilus Bacillus mesentericus AQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSSALYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSANQRASFSSAGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGSSFYYGKGLINVQAAAQ mint Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides thet_thevu Thermitase protein protein thevu Thermoactinomyces vulgaris YTPNDPYFSSRQYGPQKIQAPQAWDIAEGSGAKIAIVDTGVQSNHPDLAGKVVGGWDFVDNDSTPQNGNGHGTHCAGIAAAVTNNSTGIAGTAPKASILAVRVLDNSGSGTWTAVANGITYAADQGAKVISLSLGGTVGNSGLQQAVNYAWNKGSVVVAAAGNAGNTAPNYPAYYSNAIAVASTDQNDNKSSFSTYGSVVDVAAPGSWIYSTYPTSTYASLSGTSMATPHVAGVAGLLASQGRSASNIRAAIENTADKISGTGTYWAKGRVNAYKAVQY mint subc_bacli Subtilisin Carlsberg subC apr protein protein bacli Bacillus licheniformis MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides mint tryp_pig Trypsin protein protein pig Sus scrofa (Pig) Pig FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN mint ldti_hirme Leech-derived tryptase inhibitor C protein protein medicinal leech Hirudo medicinalis KKVCACPKILKPVCGSDGRTYANSCIARCNGVSIKSEGSCPTGILN mint Acts as an inhibitor of human tryptase, trypsin and chymotrypsin. Probably acts to block host defense mechanisms ctra-icic 100478 icic_hirme 100479 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 ctra_bovin 100480 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1acb, P00766 is chain E and P01051 is chain I Resolution 2.000 mint icic-thet 100878 icic_hirme 100479 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 thet_thevu 100880 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 2tec, P04072 is chain E and P01051 is chain I Resolution 1.980 mint apr-icic 100494 icic_hirme 100479 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 subt_bacam 100496 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1sbn, P00782 is chain E and P01051 is chain I Resolution 2.100 mint apr-icic-1 100510 icic_hirme 100479 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 subt_bacpu 100512 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1mee, P07518 is chain A and P01051 is chain I Resolution 2.000 mint ldti-tryp 101101 ldti_hirme 101102 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 tryp_pig 101103 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1ldt, P80424 is chain L and P00761 is chain T Resolution 1.900 mint apr-icic-2 100910 icic_hirme 100479 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 subt_bacli 100912 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1cse, P00780 is chain E and P01051 is chain I Resolution 1.200 mint cpa2-mcpi 100269 mcpi_hirme 100270 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 cbpa2_human 100271 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1dtd, P48052 is chain A and P81511 is chain B Resolution 1.650 mint