A Grp on the Hsp90 mechanism

Mol Cell. 2007 Oct 26;28(2):177-9. doi: 10.1016/j.molcel.2007.10.007.

Abstract

In a recent issue of Molecular Cell, Dollins et al. (2007) present the crystal structure of Grp94, which highlights the similarity between Grp94 and Hsp90 and provides insight into the resting state of Grp94 and potentially other Hsp90 family members.

Publication types

  • Comment
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism
  • Adenylyl Imidodiphosphate / metabolism
  • Animals
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallography
  • Cytoplasm / metabolism
  • Dimerization
  • Endoplasmic Reticulum / metabolism
  • HSP70 Heat-Shock Proteins / chemistry*
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / chemistry*
  • HSP90 Heat-Shock Proteins / metabolism
  • Humans
  • Hydrolysis
  • Kinetics
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Signal Transduction*

Substances

  • Bacterial Proteins
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Membrane Proteins
  • glucose-regulated proteins
  • HtpG protein, bacteria
  • Adenylyl Imidodiphosphate
  • Adenosine Diphosphate
  • Adenosine Triphosphate