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2fot

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Revision as of 09:00, 14 June 2018

Crystal structure of the complex between calmodulin and alphaII-spectrin

Structural highlights

2fot is a 2 chain structure with sequence from Bos taurus and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1cdm, 1mxe, 1iwq, 1niw
Gene:	SPTAN1, SPTA2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[SPTN1_HUMAN] West syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

[CALM_BOVIN] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). [SPTN1_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

AlphaII-spectrin is a major cortical cytoskeletal protein contributing to membrane organization and integrity. The Ca2+-activated binding of calmodulin to an unstructured insert in the 11th repeat unit of alphaII-spectrin enhances the susceptibility of spectrin to calpain cleavage but abolishes its sensitivity to several caspases and to at least one bacterially derived pathologic protease. Other regulatory inputs including phosphorylation by c-Src also modulate the proteolytic susceptibility of alphaII-spectrin. These pathways, acting through spectrin, appear to control membrane plasticity and integrity in several cell types. To provide a structural basis for understanding these crucial biological events, we have solved the crystal structure of a complex between bovine calmodulin and the calmodulin-binding domain of human alphaII-spectrin (Protein Data Bank ID code 2FOT). The structure revealed that the entire calmodulin-spectrin-binding interface is hydrophobic in nature. The spectrin domain is also unique in folding into an amphiphilic helix once positioned within the calmodulin-binding groove. The structure of this complex provides insight into the mechanisms by which calmodulin, calpain, caspase, and tyrosine phosphorylation act on spectrin to regulate essential cellular processes.

Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity.,Simonovic M, Zhang Z, Cianci CD, Steitz TA, Morrow JS J Biol Chem. 2006 Nov 10;281(45):34333-40. Epub 2006 Aug 31. PMID:16945920^[1]

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

References

↑ Simonovic M, Zhang Z, Cianci CD, Steitz TA, Morrow JS. Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. J Biol Chem. 2006 Nov 10;281(45):34333-40. Epub 2006 Aug 31. PMID:16945920 doi:http://dx.doi.org/10.1074/jbc.M604613200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fot"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex between calmodulin and alphaII-spectrin==
 <StructureSection load='2fot' size='340' side='right' caption='[[2fot]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cdm|1cdm]], [[1mxe|1mxe]], [[1iwq|1iwq]], [[1niw|1niw]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPTAN1, SPTA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2fot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fot OCA], [http://pdbe.org/2fot PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fot RCSB], [http://www.ebi.ac.uk/pdbsum/2fot PDBsum]</span></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=2fot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fot OCA], [http://pdbe.org/2fot PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fot RCSB], [http://www.ebi.ac.uk/pdbsum/2fot PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fot ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 16: / Line 17: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/2fot_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/2fot_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2fot

From Proteopedia

Revision as of 09:00, 14 June 2018

Crystal structure of the complex between calmodulin and alphaII-spectrin

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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