1dtv: Difference between revisions

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[[Image:1dtv.jpg|left|200px]]<br /><applet load="1dtv" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1dtv.jpg|left|200px]]
caption="1dtv" />
 
'''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)'''<br />
{{Structure
|PDB= 1dtv |SIZE=350|CAPTION= <scene name='initialview01'>1dtv</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1DTV is a [http://en.wikipedia.org/wiki/Single_protein 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].  
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10742178 10742178]
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]]


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Revision as of 08:44, 20 March 2008

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1dtv
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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

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