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==CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN==
==CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN==
<StructureSection load='1aa2' size='340' side='right' caption='[[1aa2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1aa2' size='340' side='right'caption='[[1aa2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1aa2]] 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=1AA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AA2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1aa2]] is a 1 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=1AA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AA2 FirstGlance]. <br>
</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=1aa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa2 OCA], [http://pdbe.org/1aa2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aa2 RCSB], [http://www.ebi.ac.uk/pdbsum/1aa2 PDBsum]</span></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&#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=1aa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa2 OCA], [https://pdbe.org/1aa2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aa2 RCSB], [https://www.ebi.ac.uk/pdbsum/1aa2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aa2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SPTB2_HUMAN SPTB2_HUMAN]] Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.  
[https://www.uniprot.org/uniprot/SPTB2_HUMAN SPTB2_HUMAN] Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/1aa2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/1aa2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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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=1aa2 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=1aa2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of the calponin homology domain present in many actin binding cytoskeletal and signal-transducing proteins has been determined at 2.0 A resolution.
Crystal structure of a calponin homology domain.,Djinovic Carugo K, Banuelos S, Saraste M Nat Struct Biol. 1997 Mar;4(3):175-9. PMID:9164454<ref>PMID:9164454</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1aa2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Spectrin|Spectrin]]
*[[Spectrin 3D structures|Spectrin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Banuelos, S]]
[[Category: Large Structures]]
[[Category: Carugo, K Djinovic]]
[[Category: Banuelos S]]
[[Category: Saraste, M]]
[[Category: Djinovic Carugo K]]
[[Category: Cytoskeleton]]
[[Category: Saraste M]]
[[Category: F-actin cross-linking]]
[[Category: Spectrin]]

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