|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
2003-4-28
|
|
pubmed:abstractText |
We report the effects of peptide binding on the (15)N relaxation rates and chemical shifts of the C-SH3 of Sem-5. (15)N spin-lattice relaxation time (T(1)), spin-spin relaxation time (T(2)), and ((1)H)-(15)N NOE were obtained from heteronuclear 2D NMR experiments. These parameters were then analyzed using the Lipari-Szabo model free formalism to obtain parameters that describe the internal motions of the protein. High-order parameters (S(2) > 0.8) are found in elements of regular secondary structure, whereas some residues in the loop regions show relatively low-order parameters, notably the RT loop. Peptide binding is characterized by a significant decrease in the (15)N relaxation in the RT loop. Concomitant with the change in dynamics is a cooperative change in chemical shifts. The agreement between the binding constants calculated from chemical shift differences and that obtained from ITC indicates that the binding of Sem-5 C-SH3 to its putative peptide ligand is coupled to a cooperative conformational change in which a portion of the binding site undergoes a significant reduction in conformational heterogeneity.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-10393272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-10421358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-10421374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-10581552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-10605085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-10739251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-10835283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-11495246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-11697910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-1280858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-1322798,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-1372395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-14268785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-2223770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-2690953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-2757186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-6615806,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7514039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7531772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7563055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7684655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7796257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7796263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7796268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7802869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7947763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-7987221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8422352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8462098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8479536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8555205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8744573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8913313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8961927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8973171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-8973173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9047330,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9100005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9461082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9485443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9521116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9566119,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9571048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9600847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12717021-9922172
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0961-8368
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
12
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
982-96
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:12717021-Binding Sites,
pubmed-meshheading:12717021-Caenorhabditis elegans Proteins,
pubmed-meshheading:12717021-Ligands,
pubmed-meshheading:12717021-Models, Molecular,
pubmed-meshheading:12717021-Motion,
pubmed-meshheading:12717021-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12717021-Peptides,
pubmed-meshheading:12717021-Protein Binding,
pubmed-meshheading:12717021-Protein Conformation,
pubmed-meshheading:12717021-src Homology Domains
|
|
pubmed:year |
2003
|
|
pubmed:articleTitle |
Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling.
|
|
pubmed:affiliation |
Department of Human Biological Chemistry and Genetics, and Sealy Center for Structural Biology, University of Texas Medical Branch at Galveston, Galveston, Texas 77555, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
