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==HUMAN ALPHAB CRYSTALLIN ACD R120G==
 
<StructureSection load='2y1z' size='340' side='right' caption='[[2y1z]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
==Human alphaB Crystallin ACD R120G==
<StructureSection load='2y1z' size='340' side='right'caption='[[2y1z]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2y1z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y1Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[2y1z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y1Z FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wj7|2wj7]], [[2y1y|2y1y]], [[2y22|2y22]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></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=2y1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y1z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y1z RCSB], [http://www.ebi.ac.uk/pdbsum/2y1z PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y1z OCA], [https://pdbe.org/2y1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y1z RCSB], [https://www.ebi.ac.uk/pdbsum/2y1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y1z ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/CRYAB_HUMAN 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.  
[https://www.uniprot.org/uniprot/CRYAB_HUMAN 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 ==
== Function ==
[[http://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 ==
Small heat shock proteins form large cytosolic assemblies from an "alpha-crystallin domain" (ACD) flanked by sequence extensions. Mutation of a conserved arginine in the ACD of several human small heat shock protein family members causes many common inherited diseases of the lens and neuromuscular system. The mutation R120G in alphaB-crystallin causes myopathy, cardiomyopathy and cataract. We have solved the X-ray structure of the excised ACD dimer of human alphaB R120G close to physiological pH and compared it with several recently determined wild-type vertebrate ACD dimer structures. Wild-type excised ACD dimers have a deep groove at the interface floored by a flat extended "bottom sheet." Solid-state NMR studies of large assemblies of full-length alphaB-crystallin have shown that the groove is blocked in the ACD dimer by curvature of the bottom sheet. The crystal structure of R120G ACD dimer also reveals a closed groove, but here the bottom sheet is flat. Loss of Arg120 results in rearrangement of an extensive array of charged interactions across this interface. His83 and Asp80 on movable arches on either side of the interface close the groove by forming two new salt bridges. The residues involved in this extended set of ionic interactions are conserved in Hsp27, Hsp20, alphaA- and alphaB-crystallin sequences. They are not conserved in Hsp22, where mutation of the equivalent of Arg120 causes neuropathy. We speculate that the alphaB R120G mutation disturbs oligomer dynamics, causing the growth of large soluble oligomers that are toxic to cells by blocking essential processes.
 
Crystal Structure of R120G Disease Mutant of Human alphaB-Crystallin Domain Dimer Shows Closure of a Groove.,Clark AR, Naylor CE, Bagneris C, Keep NH, Slingsby C J Mol Biol. 2011 Feb 15. PMID:21329698<ref>PMID:21329698</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Crystallin 3D structures|Crystallin 3D structures]]
*[[Multiple sclerosis|Multiple sclerosis]]
*[[Multiple sclerosis|Multiple sclerosis]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bagneris, C.]]
[[Category: Large Structures]]
[[Category: Clark, A R.]]
[[Category: Bagneris C]]
[[Category: Keep, N H.]]
[[Category: Clark AR]]
[[Category: Naylor, C E.]]
[[Category: Keep NH]]
[[Category: Slingsby, C.]]
[[Category: Naylor CE]]
[[Category: Cataract]]
[[Category: Slingsby C]]
[[Category: Chaperone]]
[[Category: Eye lens protein]]
[[Category: Small heat shock protein]]
[[Category: Stress protein]]

Latest revision as of 10:11, 1 May 2024

Human alphaB Crystallin ACD R120GHuman alphaB Crystallin ACD R120G

Structural highlights

2y1z is a 2 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:X-ray diffraction, Resolution 2.5Å
Ligands:,
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.

See Also

2y1z, resolution 2.50Å

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