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5a38

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Revision as of 08:18, 26 June 2019

Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle.

Structural highlights

5a38 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5a36, 5a37
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[ACTN2_HUMAN] Defects in ACTN2 are the cause of cardiomyopathy dilated type 1AA (CMD1AA) [MIM:612158]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.^[1]

Function

[ACTN2_HUMAN] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

Publication Abstract from PubMed

alpha-actinin 2 (ACTN2) is the only muscle isoform of alpha-actinin expressed in cardiac muscle. Mutations in this protein have been implicated in mild to moderate forms of hypertrophic cardiomyopathy (HCM). We have investigated the effects of two mutations identified from HCM patients; A119T and G111V, on the secondary and tertiary structure of a purified actin binding domain of ACTN2 by circular dichroism and X-ray crystallography, and show small but distinct changes for both mutations. We also find that both mutants have reduced F-actin binding affinity, although the differences are not significant. The full length mEos2 tagged protein expressed in adult cardiomyocytes shows that both mutations additionally affect Z-disc localisation and dynamic behaviour. Overall, these two mutations have small effects on structure, function and behaviour, which may contribute to a mild phenotype for this disease.

Hypertrophic Cardiomyopathy Mutations in the calponin-homology domain of ACTN2 affect actin binding and cardiomyocyte Z-disc incorporation.,Haywood N, Wolny M, Rogers B, Trinh CH, Shuping Y, Edwards TA, Peckham M Biochem J. 2016 Jun 10. pii: BCJ20160421. PMID:27287556^[2]

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

References

↑ Mohapatra B, Jimenez S, Lin JH, Bowles KR, Coveler KJ, Marx JG, Chrisco MA, Murphy RT, Lurie PR, Schwartz RJ, Elliott PM, Vatta M, McKenna W, Towbin JA, Bowles NE. Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis. Mol Genet Metab. 2003 Sep-Oct;80(1-2):207-15. PMID:14567970
↑ Haywood N, Wolny M, Rogers B, Trinh CH, Shuping Y, Edwards TA, Peckham M. Hypertrophic Cardiomyopathy Mutations in the calponin-homology domain of ACTN2 affect actin binding and cardiomyocyte Z-disc incorporation. Biochem J. 2016 Jun 10. pii: BCJ20160421. PMID:27287556 doi:http://dx.doi.org/10.1042/BCJ20160421

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5a38"

@@ Line 1: / Line 1: @@
 ==Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle.==
-<StructureSection load='5a38' size='340' side='right' caption='[[5a38]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='5a38' size='340' side='right'caption='[[5a38]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5a38]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A38 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A38 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5a38]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A38 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A38 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a36|5a36]], [[5a37|5a37]]</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=5a38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a38 OCA], [http://pdbe.org/5a38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a38 RCSB], [http://www.ebi.ac.uk/pdbsum/5a38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a38 ProSAT]</span></td></tr>
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 5a38" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Actinin 3D structures|Actinin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Edwards, T A]]
 [[Category: Haywood, N J]]

5a38

From Proteopedia

Revision as of 08:18, 26 June 2019

Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle.

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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