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1fng

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[[Image:1fng.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fng OCA], [http://www.ebi.ac.uk/pdbsum/1fng PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fng RCSB]</span>
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'''HISTOCOMPATIBILITY ANTIGEN'''
'''HISTOCOMPATIBILITY ANTIGEN'''
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[[Category: Miley, M J.]]
[[Category: Miley, M J.]]
[[Category: Nelson, C A.]]
[[Category: Nelson, C A.]]
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[[Category: histocompatibility antigen]]
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[[Category: Histocompatibility antigen]]
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[[Category: immune system]]
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[[Category: Immune system]]
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[[Category: mhc]]
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[[Category: Mhc]]
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[[Category: peptide]]
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[[Category: Peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:32:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:29 2008''
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Revision as of 13:32, 2 May 2008

Template:STRUCTURE 1fng

HISTOCOMPATIBILITY ANTIGEN


Overview

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.

About this Structure

1FNG is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural and functional consequences of altering a peptide MHC anchor residue., Kersh GJ, Miley MJ, Nelson CA, Grakoui A, Horvath S, Donermeyer DL, Kappler J, Allen PM, Fremont DH, J Immunol. 2001 Mar 1;166(5):3345-54. PMID:11207290 Page seeded by OCA on Fri May 2 16:32:12 2008

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