Authors
Dietlind L Gerloff, Fred E Cohen, Chantal Korostensky, Marcel Turcotte, Gaston H Gonnet, Steven A Benner
Publication date
1997/3
Journal
Proteins: Structure, Function, and Bioinformatics
Volume
27
Issue
3
Pages
450-458
Publisher
Wiley Subscription Services, Inc., A Wiley Company
Description
A secondary structure has been predicted for the heat shock protein HSP90 family from an aligned set of homologous protein sequences by using a transparent method in both manual and automated implementation that extracts conformational information from patterns of variation and conservation within the family. No statistically significant sequence similarity relates this family to any protein with known crystal structure. However, the secondary structure prediction, together with the assignment of active site positions and possible biochemical properties, suggest that the fold is similar to that seen in N‐terminal domain of DNA gyrase B (the ATPase fragment). Proteins 27:450–458, 1997. © 1997 Wiley‐Liss, Inc.
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DL Gerloff, FE Cohen, C Korostensky, M Turcotte… - Proteins: Structure, Function, and Bioinformatics, 1997