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A predicted consensus structure for the N‐Terminal fragment of the heat shock protein HSP90 family
Author(s) -
Gerloff Dietlind L.,
Cohen Fred E.,
Korostensky Chantal,
Turcotte Marcel,
Gonnet Gaston H.,
Benner Steven A.
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199703)27:3<450::aid-prot12>3.0.co;2-k
Subject(s) - hsp90 , heat shock protein , fragment (logic) , terminal (telecommunication) , shock (circulatory) , genetics , biology , computer science , medicine , gene , algorithm , telecommunications
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.