1dtd
From Proteopedia
(New page: 200px<br /> <applet load="1dtd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dtd, resolution 1.65Å" /> '''CRYSTAL STRUCTURE O...) |
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caption="1dtd, resolution 1.65Å" /> | caption="1dtd, resolution 1.65Å" /> | ||
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)'''<br /> | '''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Leech carboxypeptidase inhibitor (LCI) is a novel protein inhibitor | + | 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== | ||
| - | 1DTD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and GLU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1DTD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GLU:'>GLU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Peptidyl-dipeptidase A]] | [[Category: Peptidyl-dipeptidase A]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Aviles, F | + | [[Category: Aviles, F X.]] |
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Fernandez-Catalan, C.]] | [[Category: Fernandez-Catalan, C.]] | ||
| - | [[Category: Holak, T | + | [[Category: Holak, T A.]] |
[[Category: Reverter, D.]] | [[Category: Reverter, D.]] | ||
[[Category: GLU]] | [[Category: GLU]] | ||
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[[Category: leech carboxypeptidase inhibitor]] | [[Category: leech carboxypeptidase inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:19 2008'' |
Revision as of 10:20, 21 February 2008
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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 with and as ligands. Active as Peptidyl-dipeptidase A, with EC number 3.4.15.1 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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