Title : Mitotic phosphorylation regulates Hsp72 spindle localization by uncoupling ATP binding from substrate release.

Pub. Date : 2018 Aug 14

PMID : 30108182






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Hsp72 is a member of the 70-kDa heat shock family of molecular chaperones (Hsp70s) that comprise a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD) connected by a linker that couples the exchange of adenosine diphosphate (ADP) for adenosine triphosphate (ATP) with the release of the protein substrate. Adenosine Diphosphate heat shock protein family A (Hsp70) member 1A Homo sapiens
2 Hsp72 is a member of the 70-kDa heat shock family of molecular chaperones (Hsp70s) that comprise a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD) connected by a linker that couples the exchange of adenosine diphosphate (ADP) for adenosine triphosphate (ATP) with the release of the protein substrate. Adenosine Diphosphate heat shock protein family A (Hsp70) member 1A Homo sapiens