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1iwq

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Revision as of 11:07, 4 August 2021

Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin

Structural highlights

1iwq is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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 PubMed

The 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.

References

↑ Yamauchi E, Nakatsu T, Matsubara M, Kato H, Taniguchi H. Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Nat Struct Biol. 2003 Mar;10(3):226-31. PMID:12577052 doi:10.1038/nsb900

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iwq"

@@ Line 3: / Line 3: @@
 <StructureSection load='1iwq' size='340' side='right'caption='[[1iwq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[1iwq]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/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" id="ligandDat"><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://pdbe.org/1iwq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iwq RCSB], [http://www.ebi.ac.uk/pdbsum/1iwq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwq ProSAT], [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'>[https://proteopedia.org/fgij/fg.htm?mol=1iwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwq OCA], [https://pdbe.org/1iwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iwq RCSB], [https://www.ebi.ac.uk/pdbsum/1iwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwq ProSAT], [https://www.topsan.org/Proteins/RSGI/1iwq TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MARCS_MOUSE 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.
+[[https://www.uniprot.org/uniprot/MARCS_MOUSE 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1iwq

From Proteopedia

Revision as of 11:07, 4 August 2021

Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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