rdf:type |
|
lifeskim:mentions |
umls-concept:C0009015,
umls-concept:C0010423,
umls-concept:C0017262,
umls-concept:C0034790,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0439097,
umls-concept:C1514562,
umls-concept:C1547348,
umls-concept:C1552644,
umls-concept:C1705241,
umls-concept:C1823153,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2349976,
umls-concept:C2911684
|
pubmed:issue |
12
|
pubmed:dateCreated |
1997-3-19
|
pubmed:abstractText |
T-lymphocytes recognize a wide variety of antigens through highly diverse cell-surface glycoproteins known as T-cell receptors (TCRs). These disulfide-linked heterodimers are composed of alpha and beta or gamma and delta polypeptide chains consisting of variable (V) and constant (C) domains non-covalently associated with at least four invariant chains to form the TCR-CD3 complex. It is well established that alpha beta TCRs recognize antigen in the form of peptides bound to molecules of the major histocompatibility complex (MHC); furthermore, information on the three-dimensional structure of alpha beta TCRs has recently become available through X-ray crystallography. In contrast, the antigen specificity of gamma delta TCRs is much less well understood and their three-dimensional structure is unknown. We have cloned the delta chain of a human TCR specific for the MHC class I HLA-A2 molecule and expressed the V domain as a secreted protein in the periplasmic space of Escherichia coli. Following affinity purification using a nickel chelate adsorbent, the recombinant V delta domain was crystallized in a form suitable for X-ray diffraction analysis. The crystals are orthorhombic, space group P2(1)2(1)2 with unit cell dimensions a = 69.9, b = 49.0, c = 61.6 A. and diffract to beyond 2.3 A resolution. The ability of a V delta domain produced in bacteria to form well-ordered crystals strongly suggests that the periplasmic space can provide a suitable environment for the correct in vivo folding of gamma delta TCRs.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-1286869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-1315417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-1495977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-1598575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-1924326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-2111341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-2199796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-2523393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-2528071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-2677748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-2974163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-3043226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-3285471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-3413078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-3499667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-3518750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-7515113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-7701320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-7753173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-7932722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8090768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8146660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8289304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8340374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8387198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8525376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8548281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8976572-8717525
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0961-8368
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
5
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2638-42
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:8976572-Amino Acid Sequence,
pubmed-meshheading:8976572-Base Sequence,
pubmed-meshheading:8976572-Cloning, Molecular,
pubmed-meshheading:8976572-Crystallization,
pubmed-meshheading:8976572-Crystallography, X-Ray,
pubmed-meshheading:8976572-Escherichia coli,
pubmed-meshheading:8976572-Gene Expression,
pubmed-meshheading:8976572-Humans,
pubmed-meshheading:8976572-Immunoglobulin Variable Region,
pubmed-meshheading:8976572-Molecular Sequence Data,
pubmed-meshheading:8976572-Receptors, Antigen, T-Cell, gamma-delta
|
pubmed:year |
1996
|
pubmed:articleTitle |
Cloning, expression, and crystallization of the V delta domain of a human gamma delta T-cell receptor.
|
pubmed:affiliation |
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville 20850, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|