Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-10-30
pubmed:abstractText
SecB, a molecular chaperone involved in protein export in Escherichia coli, displays the remarkable ability to selectively bind many different polypeptide ligands whose only common feature is that of being nonnative. The selectivity is explained in part by a kinetic partitioning between the folding of a polypeptide and its association with SecB. SecB has no affinity for native, stably folded polypeptides but interacts tightly with polypeptides that are nonnative. In order to better understand the nature of the binding, we have examined the interaction of SecB with intermediates along the folding pathway of maltose-binding protein. Taking advantage of forms of maltose-binding protein that are altered in their folding properties, we show that the first intermediate in folding, represented by the collapsed state, binds to SecB, and that the polypeptide remains active as a ligand until it crosses the final energy barrier to attain the native state.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-1679318, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-1989077, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2002054, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2196376, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2531087, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2556381, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2644258, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2664780, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2687876, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2822394, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2848249, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-2855285, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-3016548, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-3042772, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-3049590, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-3466173, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-3526158, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-3530497, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-3891730, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-6287919, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-6403503, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-781293, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-7961726, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-8061603, http://linkedlifedata.com/resource/pubmed/commentcorrection/7549876-8407916
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanidine, http://linkedlifedata.com/resource/pubmed/chemical/Guanidines, http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SecB protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, E coli
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0961-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1118-23
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.
pubmed:affiliation
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.