2n3j

Solution Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1

spinqualitylabelsall models 2n3j Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n3j is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 10 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease HSPB1_HUMAN Autosomal dominant Charcot-Marie-Tooth disease type 2F;Distal hereditary motor neuropathy type 2. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function HSPB1_HUMAN Involved in stress resistance and actin organization. Publication Abstract from PubMed Small heat shock proteins (sHSP) are a class of ATP-independent protein chaperones found throughout nature. They share a common ability to maintain partly unfolded proteins in soluble states under cellular stress conditions. All sHSPs contain a central domain called the alpha-crystallin domain (ACD); the domain is found in all sHSPs and in no other proteins and therefore defines the family. Though most sHSPs form large, often polydisperse oligomers from varying numbers of subunits, the ACD is both necessary and sufficient for formation of a dimer, the fundamental building block for oligomers. HSPB1 (also known as Hsp27) is unique among the ten human sHSPs because it contains a Cys residue in its dimer interface. HSPB1 is highly expressed under conditions of oxidative stress and is proposed to serve as a redox-sensitive chaperone. HSPB1 residue Cys137 has been proposed to modulate function by existing in either its oxidized (disulfide) or reduced (thiol) form (Chalova et al 2014). Here we report the solution-state NMR structure of oxidized HSPB1-ACD and compare it to a previously determined crystal structure of the reduced state. Formation of the disulfide-bond across the dimer interface yields a locked dimer structure with increased accessible hydrophobic surface. In the context of full-length HSPB1 oligomers, oxidation of Cys137 is associated with enhanced ability to bind the hydrophobic dye, 8-Anilinonapthalene-1-sulfonic-acid, implying an increased ability to interact with client proteins under oxidative stress. Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1.,Rajagopal P, Liu Y, Shi L, Clouser AF, Klevit RE J Biomol NMR. 2015 Oct;63(2):223-8. doi: 10.1007/s10858-015-9973-0. Epub 2015 Aug , 5. PMID:26243512 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Protein structures

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