1iwq: Difference between revisions

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New page: left|200px<br /> <applet load="1iwq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iwq, resolution 2.00Å" /> '''Crystal Structure o...
 
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[[Image:1iwq.gif|left|200px]]<br />
[[Image:1iwq.gif|left|200px]]<br /><applet load="1iwq" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1iwq" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1iwq, resolution 2.00&Aring;" />
caption="1iwq, resolution 2.00&Aring;" />
'''Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin'''<br />
'''Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin'''<br />


==Overview==
==Overview==
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.
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.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1IWQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IWQ OCA].  
1IWQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IWQ OCA].  


==Reference==
==Reference==
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[[Category: Matsubara, M.]]
[[Category: Matsubara, M.]]
[[Category: Nakatsu, T.]]
[[Category: Nakatsu, T.]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Taniguchi, H.]]
[[Category: Taniguchi, H.]]
[[Category: Yamauchi, E.]]
[[Category: Yamauchi, E.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:35:18 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:27 2008''

Revision as of 14:16, 21 February 2008

File:1iwq.gif


1iwq, resolution 2.00Å

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

OverviewOverview

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.

DiseaseDisease

Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]

About this StructureAbout this Structure

1IWQ is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

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