1aa2: Difference between revisions

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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/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 [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://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>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata 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>


==See Also==
==See Also==
*[[Spectrin|Spectrin]]
*[[Spectrin 3D structures|Spectrin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[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]]

Latest revision as of 09:28, 7 February 2024

CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRINCALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN

Structural highlights

1aa2 is a 1 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 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

See Also

1aa2, resolution 2.00Å

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OCA