Letter to the Editor: Backbone and side chain resonance assignmentsof a TRAV14-3 mouse T cell receptor domain

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Key words: NMR assignments, T cell receptor, TRAV14-3*02;TRAJ38*01 domainBiological contextT cell receptors (TCR) are ab heterodimeric cellsurface glycoproteins expressed clonally on matureTlymphocytesbearingtheCD4orCD8coreceptormolecules. The major histocompatibility complex(MHC)-encodedclassIorclassIImolecule,whichisexpressed on the surface of antigen presenting cells(APC),bindstoanantigenicorself peptidetoforman MHC/peptide complex. The interaction of aTCR with an MHC/peptide complex initiates adiscriminatorybindingeventoftheantigen-specificT cell response, and leads to T cell activation(GermainandMargulies,1993).Ourunderstandingof the structural basis of this molecular recognitioneventhasbeengreatlyenhancedbyidentificationofpeptide motifs for binding to MHC molecules, bymeasurements of the thermodynamics of interac-tion of MHC/peptide complexes with TCR, and byX-raycrystalstructuresofanumberofMHCclassIand class II/peptide complexes, of TCR, and of alimited number of MHC/peptide/TCR complexes(Rudolphet al.,2002).Recentstructuralstudiesthatcompare X-ray structures of unliganded TCR withTCR/MHC/peptide complexes provide evidencethat conformational changes of the complemen-taritydeterminingregions(CDRs)oftheTCRplayan important role in the functional recognition ofMHC/peptide. NMR spectroscopy offers high-res-olution information concerning the solution struc-ture and real-time mobility of regions of proteins.We report here the NMR backbone and side chainresonance assignments of a TCR Va domain,TRAV14-3*02; TRAJ38*01 (previously known asVa2.6Ja38),derivedfromaTCRthathasspecificityfor the human immunodeficiency virus envelopeglycoprotein 120-derived peptide P18-I10(RGPGRAFVTI) bound to a murine MHC class Imolecule, H-2D