1997
DOI: 10.1016/s0969-2126(97)00175-5
|View full text |Cite
|
Sign up to set email alerts
|

Not just another Fab: the crystal structure of a TcR–MHC–peptide complex

Abstract: The structure of a ternary complex formed between a T-cell receptor, a major histocompatibility complex (MHC) protein and a viral peptide provides new insights into the cellular immune response. The results provide a molecular basis for understanding the development of T cells and the reactions leading to transplant rejection and autoimmunity.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
12
0

Year Published

1998
1998
2019
2019

Publication Types

Select...
6
4

Relationship

0
10

Authors

Journals

citations
Cited by 19 publications
(13 citation statements)
references
References 18 publications
1
12
0
Order By: Relevance
“…Major Histocompatibility Complex Class I (MHC-I) 1 molecules present peptides on the surface of every nucleated cell to be recognized by the T-cell receptors (TCR) of CD8 ϩ Tcells and the Killer-cell immunoglobulin-like receptors (KIR) of Natural Killer (NK) cells (1)(2)(3)(4). MHC-I ligands arise mainly from intracellular proteins and defective ribosomal products (5) that are degraded in the cytosol by the proteasome and other proteases.…”
Section: Redundancy and Complementarity Between Erap1 And Erap2 Reveamentioning
confidence: 99%
“…Major Histocompatibility Complex Class I (MHC-I) 1 molecules present peptides on the surface of every nucleated cell to be recognized by the T-cell receptors (TCR) of CD8 ϩ Tcells and the Killer-cell immunoglobulin-like receptors (KIR) of Natural Killer (NK) cells (1)(2)(3)(4). MHC-I ligands arise mainly from intracellular proteins and defective ribosomal products (5) that are degraded in the cytosol by the proteasome and other proteases.…”
Section: Redundancy and Complementarity Between Erap1 And Erap2 Reveamentioning
confidence: 99%
“…The peptide is bound in such conformation that some of its side chains are buried in binding clefts within the MHCI and some extend outwards giving the MHCI-peptide complex unique structural features depending on the sequence of the bound peptide [6]. Structural features arising from the MHCI molecule itself and the bound peptide are recognized by the TCR [7]. Successful recognition leads to further molecular interactions between surface receptors of the two cells and to the formation of a large interface between the two cells, called *Address correspondence to this author at the Protein Chemistry Laboratory, Institute of Radioisotopes and Radiodiagnostic Products, National Centre for Scientific Research "Demokritos", Aghia Paraskevi, 15310, Greece; Tel: +30-210-6503918; Fax: +30-210-6543526; E-mail: stratos@rrp.demokritos.gr the immunological synapse [8][9][10][11][12].…”
Section: Antigenic Peptides Play the Central Role In The Adaptive Immmentioning
confidence: 99%
“…3Bi). For example, the recent structures ofTCR/MHC (47) and CD8/MHC (15) complexes indicate how assemblies of non-covalent modular units can be formed. Some modules consistently appear to have their N-and C-termini at opposite ends of the structure (e.g.…”
Section: Discussionmentioning
confidence: 99%