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1yda

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[[Image:1yda.gif|left|200px]]
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{{STRUCTURE_1yda| PDB=1yda | SCENE= }}
{{STRUCTURE_1yda| PDB=1yda | SCENE= }}
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'''STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II'''
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===STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II===
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==Overview==
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The activities and structures of certain L198 variants of human carbonic anhydrase II (CAII) have been reported recently [Krebs, J. F., Rana, F., Dluhy, R. A., &amp; Fierke, C. A. (1993) Biochemistry 32, 4496-4505; Nair, S. K., &amp; Christianson, D. W. (1993) Biochemistry 32, 4506-4514]. In order to understand the structural basis of enzyme-inhibitor affinity, we now report the dissociation rate and equilibrium constants for acetazolamide and dansylamide binding to 13 variants of CAII containing substituted amino acids at position 198. These data indicate that inhibitor affinity is modulated by the hydrophobicity and charge of the 198 side chain. Furthermore, we have determined crystal structures of L198R, L198E, and L198F CAIIs complexed with the transition state analog acetazolamide. The substituted benzyl side chain of L198F CAII does not occlude the substrate association pocket, and it is therefore not surprising that this substitution has minimal effects on catalytic properties and inhibitor binding. Nevertheless, the F198 side chain undergoes a significant conformation change in order to accommodate the binding of acetazolamide; the same behavior is observed for the engineered side chain of L198R CAII. In contrast, the engineered side chain of L198E CAII does not alter its conformation upon inhibitor binding. We conclude that the mobility and hydrophobicity or residue 198 side chains affect enzyme-inhibitor (and enzyme-substrate) affinity, and these structure-function relationships are important for understanding the behavior of carbonic anhydrase isozyme III, which bears a wild-type F198 side chain.(ABSTRACT TRUNCATED AT 250 WORDS)
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{{ABSTRACT_PUBMED_7696263}}
==About this Structure==
==About this Structure==
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[[Category: Nair, S K.]]
[[Category: Nair, S K.]]
[[Category: Hydro-lyase]]
[[Category: Hydro-lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:10:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:17:05 2008''

Revision as of 09:17, 28 July 2008

Image:1yda.png

Template:STRUCTURE 1yda

STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II

Template:ABSTRACT PUBMED 7696263

About this Structure

1YDA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of inhibitor affinity to variants of human carbonic anhydrase II., Nair SK, Krebs JF, Christianson DW, Fierke CA, Biochemistry. 1995 Mar 28;34(12):3981-9. PMID:7696263

Page seeded by OCA on Mon Jul 28 12:17:05 2008

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