17494761

Source:http://linkedlifedata.com/resource/pubmed/id/17494761

Download in:

Switch to

Custom View

Named Graph Language Inference

Statements in which the resource exists as a subject.
Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0012634, umls-concept:C0033684, umls-concept:C0205102, umls-concept:C0441712, umls-concept:C1948027
pubmed:issue	20
pubmed:dateCreated	2007-5-22
pubmed:abstractText	Transcription factors and other allosteric cell signaling proteins contain a disproportionate number of domains or segments that are intrinsically disordered (ID) under native conditions. In many cases folding of these segments is coupled to binding with one or more of their interaction partners, suggesting that intrinsic disorder plays an important functional role. Despite numerous hypotheses for the role of ID domains in regulation, a mechanistic model has yet to be established that can quantitatively assess the importance of intrinsic disorder for intramolecular site-to-site communication, the hallmark property of allosteric proteins. Here, we present such a model and show that site-to-site allosteric coupling is maximized when intrinsic disorder is present in the domains or segments containing one or both of the coupled binding sites. This result not only explains the prevalence of ID domains in regulatory proteins, it also calls into question the classical mechanical view of energy propagation in proteins, which predicts that site-to-site coupling would be maximized when a well defined pathway of folded structure connects the two sites. Furthermore, in showing that the coupling mechanism conferred by intrinsic disorder is robust and independent of the network of interactions that physically link the coupled sites, unique insights are gained into the energetic ground rules that govern site-to-site communication in all proteins.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/GM-13747
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-10514373, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-10550212, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-11035796, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-11910019, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-14343300, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-14698303, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-14990997, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-15049691, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-15469262, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-15718131, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-15767576, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-15876404, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-15943980, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-16094605, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-16683749, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-16734424, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-16784220, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-16906160, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-3464944, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-5938952, http://linkedlifedata.com/resource/pubmed/commentcorrection/17494761-6544679
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7505876
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Proteins
pubmed:status	MEDLINE
pubmed:month	May
pubmed:issn	0027-8424
pubmed:author	pubmed-author:HilserVincent JVJ, pubmed-author:ThompsonE BradEB
pubmed:issnType	Print
pubmed:day	15
pubmed:volume	104
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	8311-5
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:17494761-Allosteric Regulation, pubmed-meshheading:17494761-Models, Biological, pubmed-meshheading:17494761-Protein Structure, Tertiary, pubmed-meshheading:17494761-Proteins, pubmed-meshheading:17494761-Thermodynamics
pubmed:year	2007
pubmed:articleTitle	Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
pubmed:affiliation	Department of Biochemistry and Molecular Biology, and Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555-1068, USA. vjhilser@utmb.edu
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural