1iwq: Difference between revisions
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<StructureSection load='1iwq' size='340' side='right' caption='[[1iwq]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1iwq' size='340' side='right' caption='[[1iwq]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iwq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1iwq]] is a 2 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=1IWQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IWQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1iwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iwq RCSB], [http://www.ebi.ac.uk/pdbsum/1iwq PDBsum], [http://www.topsan.org/Proteins/RSGI/1iwq TOPSAN]</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=1iwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwq OCA], [http://pdbe.org/1iwq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iwq RCSB], [http://www.ebi.ac.uk/pdbsum/1iwq PDBsum], [http://www.topsan.org/Proteins/RSGI/1iwq TOPSAN]</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 1iwq" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Kato, H]] | [[Category: Kato, H]] | ||
[[Category: Matsubara, M]] | [[Category: Matsubara, M]] | ||
Revision as of 11:56, 10 September 2015
Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/CalmodulinCrystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin
Structural highlights
Function[MARCS_MOUSE] MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein. 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 calmodulin-binding domain of myristoylated alanine-rich C kinase substrate (MARCKS), which interacts with various targets including calmodulin, actin and membrane lipids, has been suggested to function as a crosstalk point among several signal transduction pathways. We present here the crystal structure at 2 A resolution of a peptide consisting of the MARCKS calmodulin (CaM)-binding domain in complex with Ca2+-CaM. The domain assumes a flexible conformation, and the hydrophobic pocket of the calmodulin N-lobe, which is a common CaM-binding site observed in previously resolved Ca2+-CaM-target peptide complexes, is not involved in the interaction. The present structure presents a novel target-recognition mode of calmodulin and provides insight into the structural basis of the flexible interaction module of MARCKS. Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin.,Yamauchi E, Nakatsu T, Matsubara M, Kato H, Taniguchi H Nat Struct Biol. 2003 Mar;10(3):226-31. PMID:12577052[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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