1aye: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1aye.gif|left|200px]]
{{Seed}}
[[Image:1aye.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1aye|  PDB=1aye  |  SCENE=  }}  
{{STRUCTURE_1aye|  PDB=1aye  |  SCENE=  }}  


'''HUMAN PROCARBOXYPEPTIDASE A2'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_9384570}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9384570 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9384570}}


==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Zymogen]]
[[Category: Zymogen]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:50:39 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:51:40 2008''

Revision as of 14:51, 30 June 2008

File:1aye.png

Template:STRUCTURE 1aye

HUMAN PROCARBOXYPEPTIDASE A2

Template:ABSTRACT PUBMED 9384570

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

Page seeded by OCA on Mon Jun 30 17:51:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA