Source:http://linkedlifedata.com/resource/pubmed/id/11021536
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2000-10-18
|
| pubmed:databankReference | |
| pubmed:abstractText |
Fc receptors play a major role in immune defenses against pathogens and in inflammatory processes. The crystal structure of a human immunoglobulin receptor, FcgammaRIIIb, has been determined to 1.8 A resolution. The overall fold consists of two immunoglobulin-like domains with an acute interdomain hinge angle of approximately 50 degrees. Trp-113, wedged between the N-terminal D1 and the C-terminal D2 domains, appears to further restrict the hinge angle. The putative Fc binding region of the receptor carries a net positive charge complementary to the negative-charged receptor binding regions on Fc. A 1:1 binding stoichiometry between the receptor and Fc was measured by both the equilibrium and nonequilibrium size-exclusion chromatography. Two separate parallel dimers are observed in the crystal lattice, offering intriguing models for receptor aggregation.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
1074-7613
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
13
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
387-95
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:11021536-Amino Acid Sequence,
pubmed-meshheading:11021536-Binding Sites,
pubmed-meshheading:11021536-Chromatography, Gel,
pubmed-meshheading:11021536-Conserved Sequence,
pubmed-meshheading:11021536-Crystallization,
pubmed-meshheading:11021536-Crystallography, X-Ray,
pubmed-meshheading:11021536-Dimerization,
pubmed-meshheading:11021536-Extracellular Space,
pubmed-meshheading:11021536-Humans,
pubmed-meshheading:11021536-Immunoglobulin Fragments,
pubmed-meshheading:11021536-Ligands,
pubmed-meshheading:11021536-Models, Molecular,
pubmed-meshheading:11021536-Molecular Sequence Data,
pubmed-meshheading:11021536-Oligopeptides,
pubmed-meshheading:11021536-Protein Structure, Tertiary,
pubmed-meshheading:11021536-Receptors, IgG,
pubmed-meshheading:11021536-Sequence Homology, Amino Acid
|
| pubmed:year |
2000
|
| pubmed:articleTitle |
Crystal structure of the extracellular domain of a human Fc gamma RIII.
|
| pubmed:affiliation |
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77555, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|