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| [[Image:1fng.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1fng| PDB=1fng | SCENE= }} | | {{STRUCTURE_1fng| PDB=1fng | SCENE= }} |
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| '''HISTOCOMPATIBILITY ANTIGEN'''
| | ===HISTOCOMPATIBILITY ANTIGEN=== |
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| ==Overview==
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| To better understand TCR discrimination of multiple ligands, we have analyzed the crystal structures of two Hb peptide/I-E(k) complexes that differ by only a single amino acid substitution at the P6 anchor position within the peptide (E73D). Detailed comparison of multiple independently determined structures at 1.9 A resolution reveals that removal of a single buried methylene group can alter a critical portion of the TCR recognition surface. Significant variance was observed in the peptide P5-P8 main chain as well as a rotamer difference at LeuP8, approximately 10 A distal from the substitution. No significant variations were observed in the conformation of the two MHC class II molecules. The ligand alteration results in two peptide/MHC complexes that generate bulk T cell responses that are distinct and essentially nonoverlapping. For the Hb-specific T cell 3.L2, substitution reduces the potency of the ligand 1000-fold. Soluble 3.L2 TCR binds the two peptide/MHC complexes with similar affinity, although with faster kinetics. These results highlight the role of subtle variations in MHC Ag presentation on T cell activation and signaling.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11207290}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11207290 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11207290}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mhc]] | | [[Category: Mhc]] |
| [[Category: Peptide]] | | [[Category: Peptide]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:32:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:36:58 2008'' |
