Linked Life Data

10512719

Source:http://linkedlifedata.com/resource/pubmed/id/10512719

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-11-22
pubmed:abstractText
The geometric relationships between ligands and the functional groups that bind ligands in soluble ligand-protein complexes have traditionally been deduced from distance constraints between pairs of NMR active nuclei spanning the ligand-protein interface. Frequently, the steep inverse distance dependence of the nuclear Overhauser effect (NOE), from which the distance constraints are derived, makes identification of sufficient numbers of constraints difficult. In these cases the ability to supplement NOE-derived information with distance-independent angular information can be very important. Here, the observation of residual dipolar couplings from alpha-methyl mannose bound to mannose binding-protein in a dilute liquid crystalline medium has allowed the determination of a bound ligand's average orientation. The 3-fold rotational symmetry of mannose-binding protein defines its orientational tensor and obviates the need to determine experimentally the protein's average orientation. Through superimposition of ligand and protein orientational tensors we describe the binding geometry of alpha-methyl mannose bound to mannose-binding protein. This new method is of general applicability to the study of ligands bound to proteins, and it is of particular interest when neither X-ray crystallography nor NOE techniques can provide sufficient information to describe binding geometries.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-15
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex.
pubmed:affiliation
Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.