Premium
Structural aspects of serpin inhibition
Author(s) -
Schulze Andreas J.,
Huber Robert,
Bode Wolfram,
Engh Richard A.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00369-6
Subject(s) - serpin , chemistry , biochemistry , gene
The essential roles of proteins of the serpin family in many physiological processes, along with new discoveries of their unique folding properties, have attracted intense interest in recent years. Many serpins display unusual mobile behavior attributed to rearrangements of α‐helical or β‐sheet domains, whereby large scale transitions accompany a variety of functions, including inactivation. This unusual behavior was first recognized with the X‐ray structure of modified α1‐proteinase inhibitor. Subsequent experiments, including new X‐ray structures, have revealed a surprising variety of conformations which are functionally important but only partially understood. We review here experimental evidence for conformations relevant to the serpin inhibitory mechanism.