Electronic Resource
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Biophysics and Biomolecular Structure
28 (1999), S. 181-204
ISSN:
1056-8700
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Biology
,
Physics
Notes:
Abstract A significant number of exciting papain-like cysteine protease structures have been determined by crystallographic methods over the last several years. This trove of data allows for an analysis of the structural features that empower these molecules as they efficiently carry out their specialized tasks. Although the structure of the paradigm for the family, papain, has been known for twenty years, recent efforts have reaped several structures of specialized mammalian enzymes. This review first covers the commonalities of architecture and purpose of the papain-like cysteine proteases. From that broad platform, each of the lysosomal enzymes for which there is an X-ray structure (or structures) is then examined to gain an understanding of what structural features are used to customize specificity and activity. Structure-based design of inhibitors to control pathological cysteine protease activity will also be addressed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.biophys.28.1.181
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