1aye
From Proteopedia
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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 [[1]], with EC number [3.4.17.15]. 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 Oct 29 22:12:29 2007
Categories: Homo sapiens | Single protein | Aviles, F.X. | Coll, M. | Garcia-Saez, I. | Reverte, D. | Vendrell, J. | ZN | Hydrolase | Serine protease | Zymogen
