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| | ==NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)== | | ==NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)== |
| - | <StructureSection load='1dtv' size='340' side='right' caption='[[1dtv]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1dtv' size='340' side='right'caption='[[1dtv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1dtv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DTV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1dtv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTV FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtv OCA], [http://pdbe.org/1dtv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dtv RCSB], [http://www.ebi.ac.uk/pdbsum/1dtv PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtv OCA], [https://pdbe.org/1dtv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dtv RCSB], [https://www.ebi.ac.uk/pdbsum/1dtv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dtv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MCPI_HIRME MCPI_HIRME]] Tightly binding, competitive inhibitor of different types of pancreatic-like carboxypeptidases. | + | [https://www.uniprot.org/uniprot/MCPI_HIRME MCPI_HIRME] Tightly binding, competitive inhibitor of different types of pancreatic-like carboxypeptidases. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Hirudo medicinalis]] | | [[Category: Hirudo medicinalis]] |
| - | [[Category: Aviles, F X]] | + | [[Category: Large Structures]] |
| - | [[Category: Bode, W]] | + | [[Category: Aviles FX]] |
| - | [[Category: Fernandez-Catalan, C]] | + | [[Category: Bode W]] |
| - | [[Category: Holak, T A]] | + | [[Category: Fernandez-Catalan C]] |
| - | [[Category: Reverter, D]] | + | [[Category: Holak TA]] |
| - | [[Category: Hydrolase inhibitor]]
| + | [[Category: Reverter D]] |
| - | [[Category: Lci]]
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| - | [[Category: Leech carboxypeptidase inhibitor]]
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| Structural highlights
Function
MCPI_HIRME Tightly binding, competitive inhibitor of different types of pancreatic-like carboxypeptidases.
Publication Abstract from PubMed
Leech carboxypeptidase inhibitor (LCI) is a novel protein inhibitor present in the medicinal leech Hirudo medicinalis. The structures of LCI free and bound to carboxypeptidase A2 (CPA2)have been determined by NMR and X-ray crystallography, respectively. The LCI structure defines a new protein motif that comprises a five-stranded antiparallel beta-sheet and one short alpha-helix. This structure is preserved in the complex with human CPA2 in the X-ray structure, where the contact regions between the inhibitor and the protease are defined. The C-terminal tail of LCI becomes rigid upon binding the protease as shown in the NMR relaxation studies, and it interacts with the carboxypeptidase in a substrate-like manner. The homology between the C-terminal tails of LCI and the potato carboxypeptidase inhibitor represents a striking example of convergent evolution dictated by the target protease. These new structures are of biotechnological interest since they could elucidate the control mechanism of metallo-carboxypeptidases and could be used as lead compounds for the search of fibrinolytic drugs.
Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2.,Reverter D, Fernandez-Catalan C, Baumgartner R, Pfander R, Huber R, Bode W, Vendrell J, Holak TA, Aviles FX Nat Struct Biol. 2000 Apr;7(4):322-8. PMID:10742178[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Reverter D, Fernandez-Catalan C, Baumgartner R, Pfander R, Huber R, Bode W, Vendrell J, Holak TA, Aviles FX. Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. Nat Struct Biol. 2000 Apr;7(4):322-8. PMID:10742178 doi:10.1038/74092
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