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1fng
From Proteopedia
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| - | [[Image:1fng.gif|left|200px]] | + | [[Image:1fng.gif|left|200px]] |
| - | + | ||
| - | '''HISTOCOMPATIBILITY ANTIGEN''' | + | {{Structure |
| + | |PDB= 1fng |SIZE=350|CAPTION= <scene name='initialview01'>1fng</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HISTOCOMPATIBILITY ANTIGEN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FNG is a [ | + | 1FNG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNG OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11207290 11207290] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptide]] | [[Category: peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:27 2008'' |
Revision as of 09:11, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 11:11:27 2008
