Linked Life Data

12715002

Source:http://linkedlifedata.com/resource/pubmed/id/12715002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-4-25
pubmed:databankReference
pubmed:abstractText
B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACI and BAFF-R. We have determined the crystal structure of the extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 A. The cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the beta-turn and is indispensable in the binding of BAFF. The crystal structure shows that a unique dimeric contact occurs between the BAFF-R monomers in the virus-like cage complex. The extracellular domain of TACI contains two CRDs, both of which contain the DxL motif. Modeling of TACI-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1072-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
342-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12715002-Amino Acid Sequence, pubmed-meshheading:12715002-Animals, pubmed-meshheading:12715002-B-Cell Activating Factor, pubmed-meshheading:12715002-B-Cell Activation Factor Receptor, pubmed-meshheading:12715002-Conserved Sequence, pubmed-meshheading:12715002-Crystallography, X-Ray, pubmed-meshheading:12715002-Humans, pubmed-meshheading:12715002-Immunoglobulin G, pubmed-meshheading:12715002-Membrane Proteins, pubmed-meshheading:12715002-Mice, pubmed-meshheading:12715002-Models, Molecular, pubmed-meshheading:12715002-Molecular Sequence Data, pubmed-meshheading:12715002-Protein Conformation, pubmed-meshheading:12715002-Receptors, Tumor Necrosis Factor, pubmed-meshheading:12715002-Sequence Alignment, pubmed-meshheading:12715002-Sequence Homology, Amino Acid, pubmed-meshheading:12715002-Tumor Necrosis Factor-alpha
pubmed:year
2003
pubmed:articleTitle
Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation.
pubmed:affiliation
Department of Biological Science, Korea Advanced Institute of Science and Technology, Daejeon, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't