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New page: left|200px<br /><applet load="1dtv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dtv" /> '''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE ...
 
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[[Image:1dtv.jpg|left|200px]]<br /><applet load="1dtv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dtv.jpg|left|200px]]<br /><applet load="1dtv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dtv" />
caption="1dtv" />
'''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)'''<br />
'''NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)'''<br />


==Overview==
==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.
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==
==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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DTV OCA].  
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].  


==Reference==
==Reference==
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[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Aviles, F.X.]]
[[Category: Aviles, F X.]]
[[Category: Bode, W.]]
[[Category: Bode, W.]]
[[Category: Fernandez-Catalan, C.]]
[[Category: Fernandez-Catalan, C.]]
[[Category: Holak, T.A.]]
[[Category: Holak, T A.]]
[[Category: Reverter, D.]]
[[Category: Reverter, D.]]
[[Category: lci]]
[[Category: lci]]
[[Category: leech carboxypeptidase inhibitor]]
[[Category: leech carboxypeptidase inhibitor]]


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