1aye
From Proteopedia
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| - | [[Image:1aye.gif|left|200px]] | + | [[Image:1aye.gif|left|200px]] |
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| - | '''HUMAN PROCARBOXYPEPTIDASE A2''' | + | {{Structure |
| + | |PDB= 1aye |SIZE=350|CAPTION= <scene name='initialview01'>1aye</scene>, resolution 1.8Å | ||
| + | |SITE= <scene name='pdbsite=1:Subsite+S1'+ARG+145,+ASN+144,+TYR+248+Subsite+S1+ARG+127+...'>1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN PROCARBOXYPEPTIDASE A2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AYE is a [ | + | 1AYE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/9384570 9384570] |
[[Category: Carboxypeptidase A2]] | [[Category: Carboxypeptidase A2]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:53 2008'' |
Revision as of 08:03, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Carboxypeptidase A2, with EC number 3.4.17.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 procarboxypeptidases A1, B and A2, particularly of the latter. The benzylsuccinic inhibitor is able to diffuse into the active site of procarboxypeptidase A2 in the crystals. The structure of the zymogen-inhibitor complex has been solved at 2.2 A resolution. The inhibitor enters the active site through a channel formed at the interface between the pro-segment and the enzyme regions and interacts with important elements of the active site. The derived structural features explain the intrinsic activity of A1/A2 pro-enzymes for small substrates.
About this Structure
1AYE is a Single protein structure of sequence from Homo sapiens. 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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