Source:http://linkedlifedata.com/resource/pubmed/id/12627945
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
|
| pubmed:dateCreated |
2003-3-11
|
| pubmed:abstractText |
PDZ domains are protein-protein interaction modules that normally recognize short C-terminal peptides. The apparent requirement for a ligand with a free terminal carboxylate group has led to the proposal that electrostatic interactions with the terminus play a significant role in recognition. However, this model has been called into question by the more recent finding that PDZ domains can recognize some internal peptide motifs that occur within a specific secondary structure context. Although these motifs bind at the same interface, they lack a terminal charge. Here we have investigated the role of electrostatics in PDZ-mediated recognition in the mouse alpha1-syntrophin PDZ domain by examining the salt dependence of binding to both terminal and internal ligands and the effects of mutating a conserved basic residue previously proposed to play a role in electrostatic recognition. These studies indicate that direct electrostatic interactions with the peptide terminus do not play a significant energetic role in binding. Additional chemical modification studies of the peptide terminus support a model in which steric and hydrogen bonding complementarity play a primary role in recognition specificity. Peptides with a free carboxy terminus, or presented within a specific structural context, can satisfy these requirements.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/postsynaptic density proteins,
http://linkedlifedata.com/resource/pubmed/chemical/syntrophin alpha1
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0006-2960
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
18
|
| pubmed:volume |
42
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2797-805
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:12627945-Amino Acid Sequence,
pubmed-meshheading:12627945-Animals,
pubmed-meshheading:12627945-Binding Sites,
pubmed-meshheading:12627945-Calcium-Binding Proteins,
pubmed-meshheading:12627945-Conserved Sequence,
pubmed-meshheading:12627945-Hydrogen Bonding,
pubmed-meshheading:12627945-Ligands,
pubmed-meshheading:12627945-Membrane Proteins,
pubmed-meshheading:12627945-Mice,
pubmed-meshheading:12627945-Molecular Sequence Data,
pubmed-meshheading:12627945-Muscle Proteins,
pubmed-meshheading:12627945-Mutagenesis, Site-Directed,
pubmed-meshheading:12627945-Nerve Tissue Proteins,
pubmed-meshheading:12627945-Osmolar Concentration,
pubmed-meshheading:12627945-Peptide Fragments,
pubmed-meshheading:12627945-Protein Binding,
pubmed-meshheading:12627945-Protein Interaction Mapping,
pubmed-meshheading:12627945-Protein Structure, Tertiary,
pubmed-meshheading:12627945-Sequence Homology, Amino Acid,
pubmed-meshheading:12627945-Static Electricity
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| pubmed:year |
2003
|
| pubmed:articleTitle |
Role of electrostatic interactions in PDZ domain ligand recognition.
|
| pubmed:affiliation |
Program in Biological Sciences, Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94143, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|