Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P212121, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 A shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.
Structure of a new crystal form of human Hsp70 ATPase domain.,Osipiuk J, Walsh MA, Freeman BC, Morimoto RI, Joachimiak A Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1105-7. PMID:10216320[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Osipiuk J, Walsh MA, Freeman BC, Morimoto RI, Joachimiak A. Structure of a new crystal form of human Hsp70 ATPase domain. Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1105-7. PMID:10216320
