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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2006-11-29
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pubmed:abstractText |
The SPRY domain was identified originally as a sequence repeat in the dual-specificity kinase splA and ryanodine receptors and subsequently found in many other distinct proteins, including more than 70 encoded in the human genome. It is a subdomain of the B30.2/SPRY domain and is believed to function as a protein-protein interaction module. Three-dimensional structures of several B30.2/SPRY domain-containing proteins have been reported recently: murine SSB-2 in solution by NMR spectroscopy, a Drosophila SSB (GUSTAVUS), and human PRYSPRY protein by X-ray crystallography. The three structures share a core of two antiparallel beta-sheets for the B30.2/SPRY domain but show differences located mainly at one end of the beta-sandwich. Analysis of SSB-2 residues required for interactions with its intracellular ligands has provided insights into B30.2/SPRY binding specificity and identified loop residues critical for the function of this domain. We have investigated the backbone dynamics of SSB-2 by means of Modelfree analysis of its backbone (15)N relaxation parameters and carried out coarse-grained dynamics simulation of B30.2/SPRY domain-containing proteins using normal mode analysis. Translational self-diffusion coefficients of SSB-2 measured using pulsed field gradient NMR were used to confirm the monomeric state of SSB-2 in solution. These results, together with previously reported amide exchange data, highlight the underlying flexibility of the loop regions of B30.2/SPRY domain-containing proteins that have been shown to be important for protein-protein interactions. The underlying flexibility of certain regions of the B30.2/SPRY domain-containing proteins may also contribute to some apparent structural differences observed between GUSTAVUS or PRYSPRY and SSB-2.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-10545323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-10656829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-10718609,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-2690953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-481223,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-9196055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-9204703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-9218955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-9419338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-9489922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-9582341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17088318-9679296
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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 |
Dec
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2761-72
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pubmed:dateRevised |
2010-9-15
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pubmed:meshHeading |
pubmed-meshheading:17088318-Amino Acid Sequence,
pubmed-meshheading:17088318-Animals,
pubmed-meshheading:17088318-Computer Simulation,
pubmed-meshheading:17088318-DNA-Binding Proteins,
pubmed-meshheading:17088318-Diffusion,
pubmed-meshheading:17088318-Drosophila,
pubmed-meshheading:17088318-Humans,
pubmed-meshheading:17088318-Mice,
pubmed-meshheading:17088318-Models, Molecular,
pubmed-meshheading:17088318-Molecular Sequence Data,
pubmed-meshheading:17088318-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17088318-Protein Folding,
pubmed-meshheading:17088318-Protein Structure, Secondary,
pubmed-meshheading:17088318-Protein Structure, Tertiary,
pubmed-meshheading:17088318-Sequence Homology, Amino Acid
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pubmed:year |
2006
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pubmed:articleTitle |
Dynamics of the SPRY domain-containing SOCS box protein 2: flexibility of key functional loops.
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pubmed:affiliation |
The Walter and Eliza Hall Institute of Medical Research, Parkville 3050, Victoria, Australia. syao@wehi.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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