1dtv
From Proteopedia
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| - | [[Image:1dtv.jpg|left|200px]] | + | [[Image:1dtv.jpg|left|200px]] |
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| - | '''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)''' | + | {{Structure |
| + | |PDB= 1dtv |SIZE=350|CAPTION= <scene name='initialview01'>1dtv</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DTV is a [ | + | 1DTV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTV OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10742178 10742178] |
[[Category: Hirudo medicinalis]] | [[Category: Hirudo medicinalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: leech carboxypeptidase inhibitor]] | [[Category: leech carboxypeptidase inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:14 2008'' |
Revision as of 08:44, 20 March 2008
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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 Thu Mar 20 10:44:14 2008
