Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6463
pubmed:dateCreated
1994-3-24
pubmed:abstractText
The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
367
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
532-8
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:7509040-Amino Acid Sequence, pubmed-meshheading:7509040-Amino Acids, pubmed-meshheading:7509040-Animals, pubmed-meshheading:7509040-Antigens, CD15, pubmed-meshheading:7509040-CHO Cells, pubmed-meshheading:7509040-Carrier Proteins, pubmed-meshheading:7509040-Cell Adhesion, pubmed-meshheading:7509040-Cell Adhesion Molecules, pubmed-meshheading:7509040-Cricetinae, pubmed-meshheading:7509040-Crystallography, X-Ray, pubmed-meshheading:7509040-E-Selectin, pubmed-meshheading:7509040-Epidermal Growth Factor, pubmed-meshheading:7509040-Humans, pubmed-meshheading:7509040-Lectins, pubmed-meshheading:7509040-Ligands, pubmed-meshheading:7509040-Mannose-Binding Lectins, pubmed-meshheading:7509040-Models, Molecular, pubmed-meshheading:7509040-Molecular Sequence Data, pubmed-meshheading:7509040-Mutagenesis, pubmed-meshheading:7509040-Neutrophils, pubmed-meshheading:7509040-Rats, pubmed-meshheading:7509040-Structure-Activity Relationship
pubmed:year
1994
pubmed:articleTitle
Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains.
pubmed:affiliation
Roche Research Center, Hoffmann-La Roche Inc., Nutley, New Jersey 07110.
pubmed:publicationType
Journal Article