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From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CRYAB_HUMAN 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. | [https://www.uniprot.org/uniprot/CRYAB_HUMAN 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. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The small heat shock protein (sHSP) alphaB-crystallin (alphaB) plays a key role in the cellular protection system against stress. For decades, high-resolution structural studies on heterogeneous sHSPs have been confounded by the polydisperse nature of alphaB oligomers. We present an atomic-level model of full-length alphaB as a symmetric 24-subunit multimer based on solid-state NMR, small-angle X-ray scattering (SAXS), and EM data. The model builds on our recently reported structure of the homodimeric alpha-crystallin domain (ACD) and C-terminal IXI motif in the context of the multimer. A hierarchy of interactions contributes to build multimers of varying sizes: Interactions between two ACDs define a dimer, three dimers connected by their C-terminal regions define a hexameric unit, and variable interactions involving the N-terminal region define higher-order multimers. Within a multimer, N-terminal regions exist in multiple environments, contributing to the heterogeneity observed by NMR. Analysis of SAXS data allows determination of a heterogeneity parameter for this type of system. A mechanism of multimerization into higher-order asymmetric oligomers via the addition of up to six dimeric units to a 24-mer is proposed. The proposed asymmetric multimers explain the homogeneous appearance of alphaB in negative-stain EM images and the known dynamic exchange of alphaB subunits. The model of alphaB provides a structural basis for understanding known disease-associated missense mutations and makes predictions concerning substrate binding and the reported fibrilogenesis of alphaB. | ||
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| - | N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity.,Jehle S, Vollmar BS, Bardiaux B, Dove KK, Rajagopal P, Gonen T, Oschkinat H, Klevit RE Proc Natl Acad Sci U S A. 2011 Apr 19;108(16):6409-14. doi:, 10.1073/pnas.1014656108. Epub 2011 Apr 4. PMID:21464278<ref>PMID:21464278</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3j07" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Crystallin 3D structures|Crystallin 3D structures]] | *[[Crystallin 3D structures|Crystallin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
Current revision
Model of a 24mer alphaB-crystallin multimer
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Categories: Homo sapiens | Large Structures | Bardiaux B | Dove KK | Gonen T | Jehle S | Klevit RE | Oschkinat H | Rajagopal P | Vollmar B
