3znc: Difference between revisions

Revision as of 13:13, 3 July 2008

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File:3znc.png

Template:STRUCTURE 3znc

MURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDEMURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDE

Template:ABSTRACT PUBMED 9541386

About this StructureAbout this Structure

3ZNC is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination., Stams T, Chen Y, Boriack-Sjodin PA, Hurt JD, Liao J, May JA, Dean T, Laipis P, Silverman DN, Christianson DW, Protein Sci. 1998 Mar;7(3):556-63. PMID:9541386

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OCA

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-'''MURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDE'''
+===MURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDE===
-==Overview==
+<!--
-Carbonic anhydrase IV (CAIV) is a membrane-associated enzyme anchored to plasma membrane surfaces by a phosphatidylinositol glycan linkage. We have determined the 2.8-angstroms resolution crystal structure of a truncated, soluble form of recombinant murine CAIV. We have also determined the structure of its complex with a drug used for glaucoma therapy, the sulfonamide inhibitor brinzolamide (Azopt). The overall structure of murine CAIV is generally similar to that of human CAIV; however, some local structural differences are found in the active site resulting from amino acid sequence differences in the "130's segment" and the residue-63 loop (these may affect the nearby catalytic proton shuttle, His-64). Similar to human CAIV, the C-terminus of murine CAIV is surrounded by a substantial electropositive surface potential that may stabilize the interaction with the phospholipid membrane. Binding interactions observed for brinzolamide rationalize the generally weaker affinity of inhibitors used in glaucoma therapy toward CAIV compared with CAII.
+The line below this paragraph, {{ABSTRACT_PUBMED_9541386}}, adds the Publication Abstract to the page
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