1aye
From Proteopedia
(New page: 200px<br /> <applet load="1aye" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aye, resolution 1.8Å" /> '''HUMAN PROCARBOXYPEPT...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1AYE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.15 3.4.17.15]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AYE OCA]]. | + | 1AYE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Carboxypeptidase_A2 Carboxypeptidase A2]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.15 3.4.17.15]]. Structure known Active Site: 1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AYE OCA]]. |
==Reference== | ==Reference== | ||
The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen., Garcia-Saez I, Reverter D, Vendrell J, Aviles FX, Coll M, EMBO J. 1997 Dec 1;16(23):6906-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9384570 9384570] | The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen., Garcia-Saez I, Reverter D, Vendrell J, Aviles FX, Coll M, EMBO J. 1997 Dec 1;16(23):6906-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9384570 9384570] | ||
| + | [[Category: Carboxypeptidase A2]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:34:41 2007'' |
Revision as of 12:29, 30 October 2007
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HUMAN PROCARBOXYPEPTIDASE A2
Overview
The three-dimensional structure of human procarboxypeptidase A2 has been, determined using X-ray crystallography at 1.8 A resolution. This is the, first detailed structural report of a human pancreatic carboxypeptidase, and of its zymogen. Human procarboxypeptidase A2 is formed by a, pro-segment of 96 residues, which inhibits the enzyme, and a, carboxypeptidase moiety of 305 residues. The pro-enzyme maintains the, general fold when compared with other non-human counterparts. The globular, part of the pro-segment docks into the enzyme moiety and shields the S2-S4, substrate binding sites, promoting inhibition. Interestingly, important, differences are found in the pro-segment which allow the identification of, the structural determinants of the diverse activation behaviours of, ... [(full description)]
About this Structure
1AYE is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Active as [Carboxypeptidase A2], with EC number [3.4.17.15]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
Reference
The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen., Garcia-Saez I, Reverter D, Vendrell J, Aviles FX, Coll M, EMBO J. 1997 Dec 1;16(23):6906-13. PMID:9384570
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