Linked Life Data

18370588

Source:http://linkedlifedata.com/resource/pubmed/id/18370588

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-4-22
pubmed:abstractText
The cytosolic domain of human immunodeficiency virus gp160 glycoprotein contains two calmodulin-binding regions. The role of these domains in modulating intracellular calmodulin signaling is of considerable interest in unraveling the mechanism whereby calmodulin regulates Fas-mediated apoptosis in HIV-infected cells. In this investigation we have employed 2D-NMR spectroscopy to determine the solution structure of the 30-residue calmodulin-binding domain corresponding to residues 826-855 of gp160. In solution, the gp160 (826-855) peptide exhibits a high degree of segmental flexibility. Within its conformational manifold, we have detected two separate flexible amphipathic helices involving residues 826-841 and 846-855 connected by a highly flexible type-II beta-turn at Pro-843 and Arg-844. The observed NOE pattern as well as the observation of long-range NOE contacts between the side chains of His-841 and Ile-846 are compatible with the presence of this turn in the conformational manifold of this peptide. This investigation focusing on the properties of the free peptide in solution paves the way for extending the investigations on the interaction of calmodulin with HIV-1 gp160.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1931-8405
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
607-16
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Solution structure of a calmodulin-binding domain in the carboxy-terminal region of HIV type 1 gp160.
pubmed:affiliation
Comprehensive Cancer Center, CH19-B31, University of Alabama at Birmingham, Birmingham, Alabama 35294-2041, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural