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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2008-2-25
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pubmed:abstractText |
Calmodulin (CaM) binds in a Ca2+-dependent manner to the intracellular C-terminal domains of most group III metabotropic glutamate receptors (mGluRs). Here we combined mutational and biophysical approaches to define the structural basis of CaM binding to mGluR 7A. Ca2+/CaM was found to interact with mGluR 7A primarily via its C-lobe at a 1:1 CaM:C-tail stoichiometry. Pulldown experiments with mutant CaM and mGluR 7A C-tail constructs and high resolution NMR with peptides corresponding to the CaM binding region of mGluR 7A allowed us to define hydrophobic and ionic interactions required for Ca2+/CaM binding and identified a 1-8-14 CaM-binding motif. The Ca2+/CaM.mGluR 7A peptide complex displays a classical wraparound structure that closely resembles that formed by Ca2+/CaM upon binding to smooth muscle myosin light chain kinase. Our data provide insight into how Ca2+/CaM regulates group III mGluR signaling via competition with intracellular proteins for receptor-binding sites.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5577-88
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18089570-Animals,
pubmed-meshheading:18089570-Calcium,
pubmed-meshheading:18089570-Calcium Signaling,
pubmed-meshheading:18089570-Calmodulin,
pubmed-meshheading:18089570-Cell Line,
pubmed-meshheading:18089570-Humans,
pubmed-meshheading:18089570-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:18089570-Multiprotein Complexes,
pubmed-meshheading:18089570-Myosin-Light-Chain Kinase,
pubmed-meshheading:18089570-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:18089570-Protein Binding,
pubmed-meshheading:18089570-Protein Structure, Quaternary,
pubmed-meshheading:18089570-Protein Structure, Tertiary,
pubmed-meshheading:18089570-Rats,
pubmed-meshheading:18089570-Receptors, Metabotropic Glutamate,
pubmed-meshheading:18089570-Structural Homology, Protein,
pubmed-meshheading:18089570-Structure-Activity Relationship
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pubmed:year |
2008
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pubmed:articleTitle |
Structural determinants of calmodulin binding to the intracellular C-terminal domain of the metabotropic glutamate receptor 7A.
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pubmed:affiliation |
Department of Neurochemistry, Max Planck Institute for Brain Research, 60528 Frankfurt, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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