Structural highlights
Function
CELA1_PIG Acts upon elastin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mattos C, Rasmussen B, Ding X, Petsko GA, Ringe D. Analogous inhibitors of elastase do not always bind analogously. Nat Struct Biol. 1994 Jan;1(1):55-8. PMID:7656008
