Linked Life Data

11406409

Source:http://linkedlifedata.com/resource/pubmed/id/11406409

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-6-14
pubmed:abstractText
The three-dimensional structures of LG/LNS domains from neurexin, the laminin alpha 2 chain and sex hormone-binding globulin reveal a close structural relationship to the carbohydrate-binding pentraxins and other lectins. However, these LG/LNS domains appear to have a preferential ligand-interaction site distinct from the carbohydrate-binding sites found in lectins, and this interaction site accommodates not only sugars but also steroids and proteins. In fact, the LG/LNS domain interaction site has features reminiscent of the antigen-combining sites in immunoglobulins. The LG/LNS domain presents an interesting case in which the fold has remained conserved but the functional sites have evolved; consequently, making predictions of structure-function relationships on the basis of the lectin fold alone is difficult.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0968-0004
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
363-8
pubmed:dateRevised
2010-4-26
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
LG/LNS domains: multiple functions -- one business end?
pubmed:affiliation
Howard Hughes Medical Institute and Dept of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, USA. rudenko@chop.swmed.edu
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't