1znc

From Proteopedia

Revision as of 11:17, 30 October 2007

HUMAN CARBONIC ANHYDRASE IV

Overview

It has recently been demonstrated that the C-terminal deletion mutant of, recombinant human carbonic anhydrase IV (G267X CA IV) converts the, normally glycosylphosphatidylinositol-anchored enzyme into a soluble, secretory form which has the same catalytic properties as the, membrane-associated enzyme purified from human tissues. We have determined, the three-dimensional structure of the secretory form of human CA IV by, x-ray crystallographic methods to a resolution of 2.8 A. Although the zinc, binding site and the hydrophobic substrate binding pocket of CA IV are, generally similar to those of other mammalian isozymes, unique structural, differences are found elsewhere in the active site. Two disufide linkages, Cys-6-Cys-11G and Cys-23-Cys-203, stabilize the conformation of the, ... [(full description)]

About this Structure

1ZNC is a [Single protein] structure of sequence from [Homo sapiens] with SO4 and ZN as [ligands]. Active as [Carbonate dehydratase], with EC number [4.2.1.1]. Structure known Active Sites: CTA and CTB. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution., Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW, Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. PMID:8942978

Page seeded by OCA on Tue Oct 30 13:22:32 2007