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Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78

Wisniewska, Magdalena ; Karlberg, Tobias ; Lehtiö, Lari ; Johansson, Ida ; Kotenyova, Tetyana ; Moche, Martin ; Schüler, Herwig Gay, Nick

PloS one, 2010-01, Vol.5 (1), p.e8625-e8625 [Periódico revisado por pares]

United States: Public Library of Science

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Título:
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78
Autor: Wisniewska, Magdalena ; Karlberg, Tobias ; Lehtiö, Lari ; Johansson, Ida ; Kotenyova, Tetyana ; Moche, Martin ; Schüler, Herwig
Gay, Nick
Assuntos: Adenosine diphosphate ; Adenosine triphosphatase ; Adenosine Triphosphatases - chemistry ; Amino Acid Sequence ; ATPases ; Binding ; Binding proteins ; Binding sites ; Biochemistry ; Biochemistry/Protein Folding ; Biochemistry/Structural Genomics ; Bioinformatics ; Chaperones ; Conformation ; Consortia ; Crystal structure ; Crystallization ; Crystallography ; Crystallography, X-Ray ; Crystals ; DNA, Complementary ; Foreign exchange rates ; Genomics ; GRP78 protein ; Heat shock proteins ; HSP70 Heat-Shock Proteins - chemistry ; HSP70 Heat-Shock Proteins - genetics ; Hsp70 protein ; Humans ; Immunoglobulins ; Isoforms ; Medicin och hälsovetenskap ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Polypeptides ; Properties ; Protein Conformation ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Proteins ; Sequence Homology, Amino Acid ; Structure
É parte de: PloS one, 2010-01, Vol.5 (1), p.e8625-e8625
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Current address: Department of Biochemistry and Pharmacy, Åbo Akademi, Turku, Finland
Conceived and designed the experiments: MW HS. Performed the experiments: MW TK LL IJ TK MM. Analyzed the data: MW TK LL HS. Wrote the paper: MW HS.
Descrição: The 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve polypeptide remodeling events. Hsp70 proteins consist of two major functional domains: an N-terminal nucleotide binding domain (NBD) with ATPase activity, and a C-terminal substrate binding domain (SBD). We present the first crystal structures of four human Hsp70 isoforms, those of the NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. As previously with Hsp70 family members, all four proteins crystallized in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB was observed for the HSPA5-ADP complex. The structures presented here support the view that the NBDs of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the SBDs and by accessory proteins. This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.
Editor: United States: Public Library of Science
Idioma: Inglês

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Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78

Wisniewska, Magdalena ; Karlberg, Tobias ; Lehtiö, Lari ; Johansson, Ida ; Kotenyova, Tetyana ; Moche, Martin ; Schüler, Herwig Gay, Nick

United States: Public Library of Science

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