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1hci

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CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ

Structural highlights

1hci 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 2.8Å
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

BACKGROUND: Alpha-actinin is a ubiquitously expressed protein found in numerous actin structures. It consists of an N-terminal actin binding domain, a central rod domain, and a C-terminal domain and functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins. RESULTS: We report here the crystal structure of the alpha-actinin rod. The structure is a twisted antiparallel dimer that contains a conserved acidic surface. CONCLUSIONS: The novel features revealed by the structure allow prediction of the orientation of parallel and antiparallel cross-linked actin filaments in relation to alpha-actinin. The conserved acidic surface is a possible interaction site for several cytoplasmic tails of transmembrane proteins involved in the recruitment of alpha-actinin to the plasma membrane.

Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.,Ylanne J, Scheffzek K, Young P, Saraste M Structure. 2001 Jul 3;9(7):597-604. PMID:11470434^[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
↑ Ylanne J, Scheffzek K, Young P, Saraste M. Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure. 2001 Jul 3;9(7):597-604. PMID:11470434

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/1hci"

@@ Line 3: / Line 3: @@
 <StructureSection load='1hci' size='340' side='right'caption='[[1hci]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hci]] is a 2 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=1HCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hci]] 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=1HCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCI FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h8b|1h8b]], [[1quu|1quu]]</div></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]] 2.8&#8491;</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=1hci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hci OCA], [https://pdbe.org/1hci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hci RCSB], [https://www.ebi.ac.uk/pdbsum/1hci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hci ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[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 ==
+[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]]
@@ Line 33: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Saraste, M]]
+[[Category: Saraste M]]
-[[Category: Scheffzek, K]]
+[[Category: Scheffzek K]]
-[[Category: Ylanne, J]]
+[[Category: Ylanne J]]
-[[Category: Young, P]]
+[[Category: Young P]]
-[[Category: Actin-binding protein]]
-[[Category: Contractile protein]]
-[[Category: Muscle]]
-[[Category: Triple-helix coiled coil]]
 [[Category: Z-disk]]
-[[Category: Z-line]]

1hci

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF THE ROD DOMAIN OF 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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