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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...

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Related Experiment Video

Updated: May 18, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Hsp90: structure and function.

Sophie E Jackson1

  • 1Department of Chemistry, Lensfield Road, Cambridge, UK. sej13@cam.ac.uk

Topics in Current Chemistry
|September 8, 2012
PubMed
Summary
This summary is machine-generated.

Heat shock protein 90 (Hsp90) is a crucial molecular chaperone involved in cellular processes and homeostasis. Understanding its structure and mechanism is key to developing Hsp90-targeted therapies for cancer and other diseases.

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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

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Last Updated: May 18, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Heat shock protein 90 (Hsp90) is a ubiquitous molecular chaperone essential for cellular processes like signaling, survival, and homeostasis.
  • Hsp90 plays a vital role in cellular stress response and maintaining cellular balance.
  • It has emerged as a significant therapeutic target for cancer, neurodegenerative disorders, and infectious diseases.

Purpose of the Study:

  • To review structural and mechanistic studies of Hsp90.
  • To elucidate how Hsp90 interacts with its diverse client proteins and cellular pathways.
  • To provide insights into Hsp90's function for therapeutic development.

Main Methods:

  • Structural studies of Hsp90.
  • Mechanistic investigations of Hsp90's ATPase activity.
  • Analysis of cochaperone interactions and post-translational modifications.

Main Results:

  • Hsp90's ATPase activity, modulated by ATP binding and hydrolysis, is critical for its function.
  • Cochaperones regulate Hsp90's ATPase activity, dynamics, and client protein interactions.
  • Post-translational modifications like phosphorylation and acetylation further regulate Hsp90 activity.

Conclusions:

  • Hsp90's structure and mechanism are complex, involving ATPase activity, cochaperones, and regulatory modifications.
  • A thorough understanding of Hsp90 function is crucial for its therapeutic applications.
  • Further research into Hsp90's intricacies will facilitate the development of novel treatments.