1h8b
From Proteopedia
(Difference between revisions)
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==EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin== | ==EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin== | ||
| - | <StructureSection load='1h8b' size='340' side='right'caption='[[1h8b | + | <StructureSection load='1h8b' size='340' side='right'caption='[[1h8b]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1h8b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1h8b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8B FirstGlance]. <br> |
| - | </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=1h8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8b OCA], [https://pdbe.org/1h8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8b RCSB], [https://www.ebi.ac.uk/pdbsum/1h8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8b ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1h8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8b OCA], [https://pdbe.org/1h8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8b RCSB], [https://www.ebi.ac.uk/pdbsum/1h8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8b ProSAT]</span></td></tr> | ||
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h8b ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h8b ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The interaction between alpha-actinin and titin, two modular muscle proteins, is essential for sarcomere assembly. We have solved the solution structure of a complex between the calcium-insensitive C-terminal EF-hand domain of alpha-actinin-2 and the seventh Z-repeat of titin. The structure of the complex is in a semi-open conformation and closely resembles that of myosin light chains in their complexes with heavy chain IQ motifs. However, no IQ motif is present in the Z-repeat, suggesting that the semi-open conformation is a general structural solution for calcium-independent recognition of EF-hand domains. | ||
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| - | Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex.,Atkinson RA, Joseph C, Kelly G, Muskett FW, Frenkiel TA, Nietlispach D, Pastore A Nat Struct Biol. 2001 Oct;8(10):853-7. PMID:11573089<ref>PMID:11573089</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1h8b" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Actinin 3D structures|Actinin 3D structures]] | *[[Actinin 3D structures|Actinin 3D structures]] | ||
| - | *[[Titin|Titin]] | + | *[[Titin 3D structures|Titin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Atkinson | + | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Frenkiel | + | [[Category: Atkinson RA]] |
| - | [[Category: Joseph | + | [[Category: Frenkiel TA]] |
| - | [[Category: Kelly | + | [[Category: Joseph C]] |
| - | [[Category: Muskett | + | [[Category: Kelly G]] |
| - | [[Category: Nietlispach | + | [[Category: Muskett FW]] |
| - | [[Category: Pastore | + | [[Category: Nietlispach D]] |
| - | + | [[Category: Pastore A]] | |
| - | + | ||
Revision as of 11:29, 27 March 2024
EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin
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