2ygd

Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approachMolecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach

2ygd, resolution 9.40Å Show:Asymmetric Unit Biological Assembly Structural highlights 2ygd is a 24 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 9.4Å Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease CRYAB_HUMAN Posterior polar cataract;Alpha-crystallinopathy;Zonular cataract;Familial isolated dilated cardiomyopathy;Fatal infantile hypertonic myofibrillar myopathy. 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. 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 CRYAB_HUMAN May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Publication Abstract from PubMed The molecular chaperone alphaB-crystallin, the major player in maintaining the transparency of the eye lens, prevents stress-damaged and aging lens proteins from aggregation. In nonlenticular cells, it is involved in various neurological diseases, diabetes, and cancer. Given its structural plasticity and dynamics, structure analysis of alphaB-crystallin presented hitherto a formidable challenge. Here we present a pseudoatomic model of a 24-meric alphaB-crystallin assembly obtained by a triple hybrid approach combining data from cryoelectron microscopy, NMR spectroscopy, and structural modeling. The model, confirmed by cross-linking and mass spectrometry, shows that the subunits interact within the oligomer in different, defined conformations. We further present the molecular architectures of additional well-defined alphaB-crystallin assemblies with larger or smaller numbers of subunits, provide the mechanism how "heterogeneity" is achieved by a small set of defined structural variations, and analyze the factors modulating the oligomer equilibrium of alphaB-crystallin and thus its chaperone activity. Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach.,Braun N, Zacharias M, Peschek J, Kastenmuller A, Zou J, Hanzlik M, Haslbeck M, Rappsilber J, Buchner J, Weinkauf S Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20491-6. Epub 2011 Dec 5. PMID:22143763 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Crystallin 3D structures