Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

HSP82 (P02829) - Overview - Molecular Target Synopsis

Protein


HSP82, ATP-dependent molecular chaperone HSP82
UniProt P02829

Also Known as HSP82_YEAST, HSP82, HSP90

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures. Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1. Interacts directly with the substrates GCN2, HAP1 and STE11.

2WEP
YEAST HSP90 N-TERMINAL DOMAIN LI-IV MUTANT WITH ADP
RCSB/PDB
Inspect Structure
See all 3D Structures for HSP82

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
709P02829-1

Sub-cellular localization


UniProt: HSP82 is active in the following subcellular-locations: cytoplasm.
GO terms: HSP82 is active in the following subcellular-locations: cell surface, cytoplasm, cytosol, fungal-type cell wall, perinuclear region of cytoplasm, plasma membrane, protein-containing complex.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project HSP82 has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For HSP82 there are:
47 structures (67 chains) solved
35 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


HSP82 has been screened with 62 compounds (119 bioactivities), 12 compounds have bioactivities that show binding affinity of <= 500nM (21 bioactivities). (see details)