Crystal structure of a complete ternary complex of T-cell receptor, peptide-MHC, and CD4
Published 2012 View Full Article
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Title
Crystal structure of a complete ternary complex of T-cell receptor, peptide-MHC, and CD4
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 14, Pages 5405-5410
Publisher
Proceedings of the National Academy of Sciences
Online
2012-03-20
DOI
10.1073/pnas.1118801109
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- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
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- Super-resolution biomolecular crystallography with low-resolution data
- (2010) Gunnar F. Schröder et al. NATURE
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- CD4 and CD8 binding to MHC molecules primarily acts to enhance Lck delivery
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- Structural alterations in peptide–MHC recognition by self-reactive T cell receptors
- (2009) Kai W Wucherpfennig et al. CURRENT OPINION IN IMMUNOLOGY
- Germline-encoded amino acids in the αβ T-cell receptor control thymic selection
- (2009) James P. Scott-Browne et al. NATURE
- Evolutionarily Conserved Amino Acids That Control TCR-MHC Interaction
- (2008) Philippa Marrack et al. Annual Review of Immunology
- Regulation of T Cell Receptor Activation by Dynamic Membrane Binding of the CD3ɛ Cytoplasmic Tyrosine-Based Motif
- (2008) Chenqi Xu et al. CELL
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