1elb
From Proteopedia
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| , resolution 2.1Å | |||||||
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| Ligands: | , , , | ||||||
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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
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