1aa2: Difference between revisions
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<StructureSection load='1aa2' size='340' side='right' caption='[[1aa2]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1aa2' size='340' side='right' caption='[[1aa2]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1aa2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <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> | ||
</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='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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1aa2" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Banuelos, S]] | [[Category: Banuelos, S]] | ||
[[Category: Carugo, K Djinovic]] | [[Category: Carugo, K Djinovic]] | ||
Revision as of 03:24, 11 September 2015
CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRINCALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN
Structural highlights
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. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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