2ak4
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2ak4 |SIZE=350|CAPTION= <scene name='initialview01'>2ak4</scene>, resolution 2.500Å | |PDB= 2ak4 |SIZE=350|CAPTION= <scene name='initialview01'>2ak4</scene>, resolution 2.500Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=IOD:IODIDE ION'>IOD</scene> | + | |LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1zhl|1ZHL]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ak4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ak4 OCA], [http://www.ebi.ac.uk/pdbsum/2ak4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ak4 RCSB]</span> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==Overview== | ||
Unusually long major histocompatibility complex (MHC) class I-restricted epitopes are important in immunity, but their 'bulged' conformation represents a potential obstacle to alphabeta T cell receptor (TCR)-MHC class I docking. To elucidate how such recognition is achieved while still preserving MHC restriction, we have determined here the structure of a TCR in complex with HLA-B(*)3508 presenting a peptide 13 amino acids in length. This complex was atypical of TCR-peptide-MHC class I interactions, being dominated at the interface by peptide-mediated interactions. The TCR assumed two distinct orientations, swiveling on top of the centrally bulged, rigid peptide such that only limited contacts were made with MHC class I. Although the TCR-peptide recognition resembled an antibody-antigen interaction, the TCR-MHC class I contacts defined a minimal 'generic footprint' of MHC-restriction. Thus our findings simultaneously demonstrate the considerable adaptability of the TCR and the 'shape' of MHC restriction. | Unusually long major histocompatibility complex (MHC) class I-restricted epitopes are important in immunity, but their 'bulged' conformation represents a potential obstacle to alphabeta T cell receptor (TCR)-MHC class I docking. To elucidate how such recognition is achieved while still preserving MHC restriction, we have determined here the structure of a TCR in complex with HLA-B(*)3508 presenting a peptide 13 amino acids in length. This complex was atypical of TCR-peptide-MHC class I interactions, being dominated at the interface by peptide-mediated interactions. The TCR assumed two distinct orientations, swiveling on top of the centrally bulged, rigid peptide such that only limited contacts were made with MHC class I. Although the TCR-peptide recognition resembled an antibody-antigen interaction, the TCR-MHC class I contacts defined a minimal 'generic footprint' of MHC-restriction. Thus our findings simultaneously demonstrate the considerable adaptability of the TCR and the 'shape' of MHC restriction. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 41: | Line 41: | ||
[[Category: Whisstock, J C.]] | [[Category: Whisstock, J C.]] | ||
[[Category: Wilce, M C.]] | [[Category: Wilce, M C.]] | ||
| - | [[Category: IOD]] | ||
[[Category: bulged epitope]] | [[Category: bulged epitope]] | ||
[[Category: pmhc/tcr complex]] | [[Category: pmhc/tcr complex]] | ||
[[Category: t cell receptor]] | [[Category: t cell receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:46 2008'' |
Revision as of 22:53, 30 March 2008
| |||||||
| , resolution 2.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1ZHL
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide
Overview
Unusually long major histocompatibility complex (MHC) class I-restricted epitopes are important in immunity, but their 'bulged' conformation represents a potential obstacle to alphabeta T cell receptor (TCR)-MHC class I docking. To elucidate how such recognition is achieved while still preserving MHC restriction, we have determined here the structure of a TCR in complex with HLA-B(*)3508 presenting a peptide 13 amino acids in length. This complex was atypical of TCR-peptide-MHC class I interactions, being dominated at the interface by peptide-mediated interactions. The TCR assumed two distinct orientations, swiveling on top of the centrally bulged, rigid peptide such that only limited contacts were made with MHC class I. Although the TCR-peptide recognition resembled an antibody-antigen interaction, the TCR-MHC class I contacts defined a minimal 'generic footprint' of MHC-restriction. Thus our findings simultaneously demonstrate the considerable adaptability of the TCR and the 'shape' of MHC restriction.
About this Structure
2AK4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide., Tynan FE, Burrows SR, Buckle AM, Clements CS, Borg NA, Miles JJ, Beddoe T, Whisstock JC, Wilce MC, Silins SL, Burrows JM, Kjer-Nielsen L, Kostenko L, Purcell AW, McCluskey J, Rossjohn J, Nat Immunol. 2005 Nov;6(11):1114-22. Epub 2005 Sep 25. PMID:16186824
Page seeded by OCA on Mon Mar 31 01:53:46 2008
Categories: Homo sapiens | Protein complex | Beddoe, T. | Borg, N A. | Buckle, A M. | Burrows, J M. | Burrows, S R. | Clements, C S. | Kjer-Nielsen, L. | Konstenko, L. | McCluskey, J. | Miles, J J. | Purcell, A W. | Rossjohn, J. | Silins, S L. | Tynan, F E. | Whisstock, J C. | Wilce, M C. | Bulged epitope | Pmhc/tcr complex | T cell receptor
