The X-ray crystal structure of a Vα2.6Jα38 mouse T cell receptor domain at 2.5 å resolution: alternate modes of dimerization and crystal packing
- 25 June 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 289 (5) , 1153-1161
- https://doi.org/10.1006/jmbi.1999.2855
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Three-dimensional structure of H-2Dd complexed with an immunodominant peptide from human immunodeficiency virus envelope glycoprotein 120Journal of Molecular Biology, 1998
- Identification of a common docking topology with substantial variation among different TCR–peptide–MHC complexesCurrent Biology, 1998
- Dual conformations of a T cell receptor Vα homodimer: implications for variability in VαVβ domain associationJournal of Molecular Biology, 1997
- Structure and function of the T-cell receptor: insights from X-ray crystallographyImmunology Today, 1996
- Biophysical studies of T-cell receptors and their ligandsCurrent Opinion in Immunology, 1996
- Kinetics of T-cell receptor binding to peptide/I-Ek complexes: correlation of the dissociation rate with T-cell responsiveness.Proceedings of the National Academy of Sciences, 1994
- Signal transduction by lymphocyte antigen receptorsCell, 1994
- SETOR: Hardware-lighted three-dimensional solid model representations of macromoleculesJournal of Molecular Graphics, 1993
- Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolutionJournal of Molecular Biology, 1991
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977