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PDBsum entry 1kb5

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Complex (immunoglobulin/receptor) PDB id
1kb5
Contents
Protein chains
115 a.a. *
117 a.a. *
214 a.a. *
219 a.a. *
Waters ×266
* Residue conservation analysis

References listed in PDB file
Key reference
Title The three-Dimensional structure of a t-Cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the v beta domain.
Authors D.Housset, G.Mazza, C.Grégoire, C.Piras, B.Malissen, J.C.Fontecilla-Camps.
Ref. EMBO J, 1997, 16, 4205-4216. [DOI no: 10.1093/emboj/16.14.4205]
PubMed id 9250664
Abstract
The crystal structure of a mouse T-cell antigen receptor (TCR) Fv fragment complexed to the Fab fragment of a specific anti-clonotypic antibody has been determined to 2.6 A resolution. The polypeptide backbone of the TCR V alpha domain is very similar to those of other crystallographically determined V alphas, whereas the V beta structure is so far unique among TCR V beta domains in that it displays a switch of the c" strand from the inner to the outer beta-sheet. The beta chain variable region of this TCR antigen-binding site is characterized by a rather elongated third complementarity-determining region (CDR3beta) that packs tightly against the CDR3 loop of the alpha chain, without leaving any intervening hydrophobic pocket. Thus, the conformation of the CDR loops with the highest potential diversity distinguishes the structure of this TCR antigen-binding site from those for which crystallographic data are available. On the basis of all these results, we infer that a significant conformational change of the CDR3beta loop found in our TCR is required for binding to its cognate peptide-MHC ligand.
Figure 3.
Figure 3 Stereoscopic view of the KB5-C20 V -V interface. The V and V domains are on the left and right sides, respectively. Only side chains of residues involved in interdomain interactions are shown. Residues are colour-coded according to their chemical nature. Acidic residues are red, basic residues dark blue, polar residues light blue, hydrophobic residues yellow and aromatic residues purple.
Figure 7.
Figure 7 Stereo pairs of the electron density map of the model contoured at the level, and generated from SIGMAA-weighted 2mF[o]-DF[c] coefficients (Read, 1986). (A) The switched c" strand and the d strand of the V domain are shown to illustrate their extended interactions. (B) The CDR3 loop is very well defined in the electron density map.
The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1997, 16, 4205-4216) copyright 1997.
Secondary reference #1
Title An alphabeta t cell receptor structure at 2.5 a and its orientation in the tcr-Mhc complex.
Authors K.C.Garcia, M.Degano, R.L.Stanfield, A.Brunmark, M.R.Jackson, P.A.Peterson, L.Teyton, I.A.Wilson.
Ref. Science, 1996, 274, 209-219.
PubMed id 8824178
Abstract
Secondary reference #2
Title Structure of the complex between human t-Cell receptor, Viral peptide and hla-A2.
Authors D.N.Garboczi, P.Ghosh, U.Utz, Q.R.Fan, W.E.Biddison, D.C.Wiley.
Ref. Nature, 1996, 384, 134-141.
PubMed id 8906788
Abstract
Secondary reference #3
Title Crystal structure of the beta chain of a t cell antigen receptor.
Authors G.A.Bentley, G.Boulot, K.Karjalainen, R.A.Mariuzza.
Ref. Science, 1995, 267, 1984-1987. [DOI no: 10.1126/science.7701320]
PubMed id 7701320
Full text Abstract
Secondary reference #4
Title Crystal structure of the V alpha domain of a t cell antigen receptor.
Authors B.A.Fields, B.Ober, E.L.Malchiodi, M.I.Lebedeva, B.C.Braden, X.Ysern, J.K.Kim, X.Shao, E.S.Ward, R.A.Mariuzza.
Ref. Science, 1995, 270, 1821-1824. [DOI no: 10.1126/science.270.5243.1821]
PubMed id 8525376
Full text Abstract
Secondary reference #5
Title Engineered secreted t-Cell receptor alpha beta heterodimers.
Authors C.Grégoire, N.Rebaï, F.Schweisguth, A.Necker, G.Mazza, N.Auphan, A.Millward, A.M.Schmitt-Verhulst, B.Malissen.
Ref. Proc Natl Acad Sci U S A, 1991, 88, 8077-8081. [DOI no: 10.1073/pnas.88.18.8077]
PubMed id 1716770
Full text Abstract
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