1dtd: Difference between revisions

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[[Image:1dtd.gif|left|200px]]
[[Image:1dtd.gif|left|200px]]


{{Structure
<!--
|PDB= 1dtd |SIZE=350|CAPTION= <scene name='initialview01'>1dtd</scene>, resolution 1.65&Aring;
The line below this paragraph, containing "STRUCTURE_1dtd", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1dtd| PDB=1dtd  | SCENE= }}  
|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>
}}


'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)'''
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)'''
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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 Fri May  2 14:15:02 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:16 2008''

Revision as of 14:15, 2 May 2008

File:1dtd.gif

Template:STRUCTURE 1dtd

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)


OverviewOverview

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 StructureAbout this Structure

1DTD is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 14:15:02 2008

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