Analogous inhibitors of elastase do not always bind analogously. Academic Article uri icon

Overview

abstract

  • 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.

publication date

  • January 1, 1994

Research

keywords

  • Pancreatic Elastase

Identity

Scopus Document Identifier

  • 0028367343

Digital Object Identifier (DOI)

  • 10.1038/nsb0194-55

PubMed ID

  • 7656008

Additional Document Info

volume

  • 1

issue

  • 1