This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2n0k

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:25, 9 March 2017

Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5

Structural highlights

2n0k is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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

Small heat shock proteins (sHSPs) are essential 'holdase' chaperones that form large assemblies and respond dynamically to pH and temperature stresses to protect client proteins from aggregation. While the alpha-crystallin domain (ACD) dimer of sHSPs is the universal building block, how the ACD transmits structural changes in response to stress to promote holdase activity is unknown. We found that the dimer interface of HSPB5 is destabilized over physiological pHs and a conserved histidine (His-104) controls interface stability and oligomer structure in response to acidosis. Destabilization by pH or His-104 mutation shifts the ACD from dimer to monomer but also results in a large expansion of HSPB5 oligomer states. Remarkably, His-104 mutant-destabilized oligomers are efficient holdases that reorganize into structurally distinct client-bound complexes. Our data support a model for sHSP function wherein cell stress triggers small perturbations that alter the ACD building blocks to unleash a cryptic mode of chaperone action.

A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis.,Rajagopal P, Tse E, Borst AJ, Delbecq SP, Shi L, Southworth DP, Klevit RE Elife. 2015 May 11;4. doi: 10.7554/eLife.07304. PMID:25962097^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rajagopal P, Tse E, Borst AJ, Delbecq SP, Shi L, Southworth DP, Klevit RE. A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. Elife. 2015 May 11;4. doi: 10.7554/eLife.07304. PMID:25962097 doi:http://dx.doi.org/10.7554/eLife.07304

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2n0k"

@@ Line 1: / Line 1: @@
 ==Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5==
 <StructureSection load='2n0k' size='340' side='right' caption='[[2n0k]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2n0k]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N0K FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2n0k RCSB], [http://www.ebi.ac.uk/pdbsum/2n0k PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0k OCA], [http://pdbe.org/2n0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n0k RCSB], [http://www.ebi.ac.uk/pdbsum/2n0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0k ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2n0k" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2n0k

From Proteopedia

Revision as of 08:25, 9 March 2017

Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox