Literature summary for 3.6.4.10 extracted from

Wisniewska, M.; Karlberg, T.; Lehtioe, L.; Johansson, I.; Kotenyova, T.; Moche, M.; Schueler, H.
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B, and HSPA5/BiP/GRP78 (2010), PLoS ONE, 5, e8625.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of four human Hsp70 isoforms are presented: nucleotide binding domains NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. All four proteins crystallize in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB is observed for the HSPA5-ADP complex. The structures presented support the view that the nucleotide binding domains of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the substrate binding domains and by accessory proteins	Homo sapiens

Crystallization (Comment)

Organism

crystal structures of four human Hsp70 isoforms are presented: nucleotide binding domains NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. All four proteins crystallize in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB is observed for the HSPA5-ADP complex. The structures presented support the view that the nucleotide binding domains of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the substrate binding domains and by accessory proteins

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
HSPA1L	-	Homo sapiens

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Release 2023.1 (January 2023)