1elb: Difference between revisions

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[[Image:1elb.~~gif~~|left|200px]]

[[Image:1elb.png|left|200px]]

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~~'''~~ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY~~'''~~

===ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY===

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_7656008}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7656008 is the PubMed ID number.

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==About this Structure==

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[[Category: Rasmussen, B.]]

[[Category: Ringe, D.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:14:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:55:55 2008''

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-[[Image:1elb.gif|left|200px]]
+{{Seed}}
+[[Image:1elb.png|left|200px]]
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 {{STRUCTURE_1elb|  PDB=1elb  |  SCENE=  }}
-'''ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY'''
+===ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7656008}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7656008 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7656008}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Rasmussen, B.]]
 [[Category: Ringe, D.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:14:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:55:55 2008''