1dtv

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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1dtv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dtv RCSB]</span>
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'''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)'''
'''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)'''
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[[Category: Holak, T A.]]
[[Category: Holak, T A.]]
[[Category: Reverter, D.]]
[[Category: Reverter, D.]]
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[[Category: lci]]
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[[Category: Lci]]
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[[Category: leech carboxypeptidase inhibitor]]
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[[Category: Leech carboxypeptidase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:32 2008''
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Revision as of 11:16, 2 May 2008

Template:STRUCTURE 1dtv

NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)


Overview

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.

About this Structure

1DTV is a Single protein structure of sequence from Hirudo medicinalis. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 14:16:02 2008

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