3sgn

From Proteopedia

(Difference between revisions)

Revision as of 07:55, 29 June 2022

Bromoderivative-8 of amyloid-related segment of alphaB-crystallin residues 90-100

Structural highlights

3sgn is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	3sgm, 3sgo, 3sgp, 3sgr, 3sgs
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

Amyloid diseases, including Alzheimer's, Parkinson's, and the prion conditions, are each associated with a particular protein in fibrillar form. These amyloid fibrils were long suspected to be the disease agents, but evidence suggests that smaller, often transient and polymorphic oligomers are the toxic entities. Here, we identify a segment of the amyloid-forming protein alphaB crystallin, which forms an oligomeric complex exhibiting properties of other amyloid oligomers: beta-sheet-rich structure, cytotoxicity, and recognition by an oligomer-specific antibody. The x-ray-derived atomic structure of the oligomer reveals a cylindrical barrel, formed from six antiparallel protein strands, that we term a cylindrin. The cylindrin structure is compatible with a sequence segment from the beta-amyloid protein of Alzheimer's disease. Cylindrins offer models for the hitherto elusive structures of amyloid oligomers.

Atomic view of a toxic amyloid small oligomer.,Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D Science. 2012 Mar 9;335(6073):1228-31. PMID:22403391^[1]

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

References

↑ Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D. Atomic view of a toxic amyloid small oligomer. Science. 2012 Mar 9;335(6073):1228-31. PMID:22403391 doi:10.1126/science.1213151

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/3sgn"

@@ Line 1: / Line 1: @@
 ==Bromoderivative-8 of amyloid-related segment of alphaB-crystallin residues 90-100==
-<StructureSection load='3sgn' size='340' side='right' caption='[[3sgn]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
+<StructureSection load='3sgn' size='340' side='right'caption='[[3sgn]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sgn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SGN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SGN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sgn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SGN FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=A8E:(2S)-2-AMINO-4-BROMOPENT-4-ENOIC+ACID'>A8E</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sgm|3sgm]], [[3sgo|3sgo]], [[3sgp|3sgp]], [[3sgr|3sgr]], [[3sgs|3sgs]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sgm|3sgm]], [[3sgo|3sgo]], [[3sgp|3sgp]], [[3sgr|3sgr]], [[3sgs|3sgs]]</div></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=3sgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sgn OCA], [http://pdbe.org/3sgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sgn RCSB], [http://www.ebi.ac.uk/pdbsum/3sgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sgn ProSAT]</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=3sgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sgn OCA], [https://pdbe.org/3sgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sgn RCSB], [https://www.ebi.ac.uk/pdbsum/3sgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sgn ProSAT]</span></td></tr>
 </table>
 == 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 ==
-[[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 ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Cascio, D]]
 [[Category: Eisenberg, D]]

3sgn

From Proteopedia

Revision as of 07:55, 29 June 2022

Bromoderivative-8 of amyloid-related segment of alphaB-crystallin residues 90-100

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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