Literature DB >> 9094746

A predicted consensus structure for the N-terminal fragment of the heat shock protein HSP90 family.

D L Gerloff1, F E Cohen, C Korostensky, M Turcotte, G H Gonnet, S A Benner.   

Abstract

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).

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Year:  1997        PMID: 9094746

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  2 in total

1.  Structural models for the protein family characterized by gamete surface protein Pfs230 of Plasmodium falciparum.

Authors:  Dietlind L Gerloff; Alison Creasey; Siarhei Maslau; Richard Carter
Journal:  Proc Natl Acad Sci U S A       Date:  2005-09-09       Impact factor: 11.205

2.  ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.

Authors:  B Panaretou; C Prodromou; S M Roe; R O'Brien; J E Ladbury; P W Piper; L H Pearl
Journal:  EMBO J       Date:  1998-08-17       Impact factor: 11.598

  2 in total

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