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1elb

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{{STRUCTURE_1elb| PDB=1elb | SCENE= }}
{{STRUCTURE_1elb| PDB=1elb | SCENE= }}
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'''ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY'''
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===ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY===
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==Overview==
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It has been assumed that the structure of a single inhibitor complex is sufficient to define the available subsites of an enzyme that has a unique binding site and a uniquely defined mode for ligand binding--the specificity for these subsites can thus be probed by kinetic experiments. Elastase is an enzyme for which these traditional assumptions, which underlie such structural and kinetic studies, do not hold. Three new crystal structures of elastase complexed to chemically similar inhibitors with similar binding affinities reveal a diversity of binding modes as well as two new subsites on elastase. The existence of multiple binding sites and different binding modes for such similar inhibitors indicates that researchers must proceed with caution when using kinetics to map out protein subsites.
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{{ABSTRACT_PUBMED_7656008}}
==About this Structure==
==About this Structure==
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[[Category: Rasmussen, B.]]
[[Category: Rasmussen, B.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:55:55 2008''

Revision as of 21:55, 30 June 2008

Image:1elb.png

Template:STRUCTURE 1elb

ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY

Template:ABSTRACT PUBMED 7656008

About this Structure

1ELB is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Analogous inhibitors of elastase do not always bind analogously., Mattos C, Rasmussen B, Ding X, Petsko GA, Ringe D, Nat Struct Biol. 1994 Jan;1(1):55-8. PMID:7656008

Page seeded by OCA on Tue Jul 1 00:55:55 2008

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