1lek
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1lek.jpg|left|200px]] | + | [[Image:1lek.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal Structure of H-2Kbm3 bound to dEV8''' | + | {{Structure |
| + | |PDB= 1lek |SIZE=350|CAPTION= <scene name='initialview01'>1lek</scene>, resolution 2.15Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of H-2Kbm3 bound to dEV8''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LEK is a [ | + | 1LEK 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=1LEK OCA]. |
==Reference== | ==Reference== | ||
| - | Structural comparison of allogeneic and syngeneic T cell receptor-peptide-major histocompatibility complex complexes: a buried alloreactive mutation subtly alters peptide presentation substantially increasing V(beta) Interactions., Luz JG, Huang M, Garcia KC, Rudolph MG, Apostolopoulos V, Teyton L, Wilson IA, J Exp Med. 2002 May 6;195(9):1175-86. PMID:[http:// | + | Structural comparison of allogeneic and syngeneic T cell receptor-peptide-major histocompatibility complex complexes: a buried alloreactive mutation subtly alters peptide presentation substantially increasing V(beta) Interactions., Luz JG, Huang M, Garcia KC, Rudolph MG, Apostolopoulos V, Teyton L, Wilson IA, J Exp Med. 2002 May 6;195(9):1175-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11994422 11994422] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 24: | Line 33: | ||
[[Category: mhc class i allogeneic complex with peptide]] | [[Category: mhc class i allogeneic complex with 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 12:30:02 2008'' |
Revision as of 10:30, 20 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of H-2Kbm3 bound to dEV8
Overview
The crystal structures of the 2C/H-2K(bm3)-dEV8 allogeneic complex at 2.4 A and H-2K(bm3)-dEV8 at 2.15 A, when compared with their syngeneic counterparts, elucidate structural changes that induce an alloresponse. The Asp77Ser mutation that imbues H-2K(bm3)-dEV8 with its alloreactive properties is located beneath the peptide and does not directly contact the T cell receptor (TCR). However, the buried mutation induces local rearrangement of the peptide itself to preserve hydrogen bonding interactions between the peptide and the alpha(1) 77 residue. The COOH terminus of the peptide main chain is tugged toward the alpha(1)-helix such that its presentation to the TCR is altered. These changes increase the stability of the allogeneic peptide-major histocompatibility complex (pMHC) complex and increase complementarity in the TCR-pMHC interface, placing greater emphasis on recognition of the pMHC by the TCR beta-chain, evinced by an increase in shape complementarity, buried surface area, and number of TCR-pMHC contacting residues. A nearly fourfold increase in the number of beta-chain-pMHC contacts is accompanied by a concomitant 64% increase in beta-chain-pMHC shape complementarity. Thus, the allogeneic mutation causes the same peptide to be presented differently, temporally and spatially, by the allogeneic and syngeneic MHCs.
About this Structure
1LEK is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural comparison of allogeneic and syngeneic T cell receptor-peptide-major histocompatibility complex complexes: a buried alloreactive mutation subtly alters peptide presentation substantially increasing V(beta) Interactions., Luz JG, Huang M, Garcia KC, Rudolph MG, Apostolopoulos V, Teyton L, Wilson IA, J Exp Med. 2002 May 6;195(9):1175-86. PMID:11994422
Page seeded by OCA on Thu Mar 20 12:30:02 2008
