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Article

Crystal structures of high affinity human T-cell receptors bound to peptide major histocompatibility complex reveal native diagonal binding geometry.

Protein engineering, design & selection : PEDS - 1 Aug 2007

Sami Malkit, Rizkallah Pierre J, Dunn Steve, Molloy Peter, Moysey Ruth, Vuidepot Annelise, Baston Emma, Todorov Penio, Li Yi, Gao Feng, Boulter Jonathan M, Jakobsen Bent K

Abstract excerpt

Naturally selected T-cell receptors (TCRs) are characterised by low binding affinities, typically in the range 1-100 microM. Crystal structures of syngeneic TCRs bound to peptide major histocompatibility complex (pMHC) antigens exhibit a conserved mode of binding characterised by a distinct diagonal binding geometry, with poor shape complementarity (SC) between receptor and ligand. Here, we report the structures...

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Share to Complementarity Determining Regions
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Structure, Secondary

Share to Receptors, Antigen, T-Cell

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Source

Identifiers

PMID: 17644531
DOI: 10.1093/protein/gzm033

Genes

CDR2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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