1quu

From Proteopedia

(Difference between revisions)

Revision as of 12:09, 27 April 2022

CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ

Structural highlights

1quu is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments.

Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments.,Djinovic-Carugo K, Young P, Gautel M, Saraste M Cell. 1999 Aug 20;98(4):537-46. PMID:10481917^[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
↑ Djinovic-Carugo K, Young P, Gautel M, Saraste M. Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell. 1999 Aug 20;98(4):537-46. PMID:10481917

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1quu"

@@ Line 3: / Line 3: @@
 <StructureSection load='1quu' size='340' side='right'caption='[[1quu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1quu]] is a 1 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=1QUU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QUU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1quu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUU FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1quu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1quu OCA], [http://pdbe.org/1quu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1quu RCSB], [http://www.ebi.ac.uk/pdbsum/1quu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1quu ProSAT]</span></td></tr>
+</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=1quu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1quu OCA], [https://pdbe.org/1quu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1quu RCSB], [https://www.ebi.ac.uk/pdbsum/1quu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1quu ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/ACTN2_HUMAN ACTN2_HUMAN]] Defects in ACTN2 are the cause of cardiomyopathy dilated type 1AA (CMD1AA) [MIM:[http://omim.org/entry/612158 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.<ref>PMID:14567970</ref>
+[[https://www.uniprot.org/uniprot/ACTN2_HUMAN ACTN2_HUMAN]] Defects in ACTN2 are the cause of cardiomyopathy dilated type 1AA (CMD1AA) [MIM:[https://omim.org/entry/612158 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.<ref>PMID:14567970</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACTN2_HUMAN ACTN2_HUMAN]] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
+[[https://www.uniprot.org/uniprot/ACTN2_HUMAN ACTN2_HUMAN]] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1quu

From Proteopedia

Revision as of 12:09, 27 April 2022

CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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