1dtd: Difference between revisions
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|PDB= 1dtd |SIZE=350|CAPTION= <scene name='initialview01'>1dtd</scene>, resolution 1.65Å | |PDB= 1dtd |SIZE=350|CAPTION= <scene name='initialview01'>1dtd</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Peptidyl-dipeptidase_A Peptidyl-dipeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.15.1 3.4.15.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidyl-dipeptidase_A Peptidyl-dipeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.15.1 3.4.15.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtd OCA], [http://www.ebi.ac.uk/pdbsum/1dtd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dtd RCSB]</span> | |||
}} | }} | ||
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[[Category: Holak, T A.]] | [[Category: Holak, T A.]] | ||
[[Category: Reverter, D.]] | [[Category: Reverter, D.]] | ||
[[Category: carboxypeptidase a2]] | [[Category: carboxypeptidase a2]] | ||
[[Category: leech carboxypeptidase inhibitor]] | [[Category: leech carboxypeptidase inhibitor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:16 2008'' | ||
Revision as of 16:48, 30 March 2008
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| 1dtd, resolution 1.65Å | |||||||||||||
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| Ligands: | GLU, ZN | ||||||||||||
| Activity: | Peptidyl-dipeptidase A, with EC number 3.4.15.1 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)
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
1DTD is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. 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
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