1aa2: Difference between revisions

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</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://www.rcsb.org/pdb/explore.do?structureId=1aa2 RCSB], [http://www.ebi.ac.uk/pdbsum/1aa2 PDBsum]</span></td></tr>
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== 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 11:18, 25 December 2014

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.
Resources:FirstGlance, OCA, RCSB, PDBsum

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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Djinovic Carugo K, Banuelos S, Saraste M. Crystal structure of a calponin homology domain. Nat Struct Biol. 1997 Mar;4(3):175-9. PMID:9164454

1aa2, resolution 2.00Å

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