2ak4: Difference between revisions

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New page: left|200px<br /> <applet load="2ak4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ak4, resolution 2.500Å" /> '''Crystal Structure ...
 
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[[Image:2ak4.gif|left|200px]]<br />
[[Image:2ak4.gif|left|200px]]<br /><applet load="2ak4" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2ak4" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2ak4, resolution 2.500&Aring;" />
caption="2ak4, resolution 2.500&Aring;" />
'''Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide'''<br />
'''Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide'''<br />


==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==
==Disease==
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==About this Structure==
==About this Structure==
2AK4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with IOD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AK4 OCA].  
2AK4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=IOD:'>IOD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AK4 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Beddoe, T.]]
[[Category: Beddoe, T.]]
[[Category: Borg, N.A.]]
[[Category: Borg, N A.]]
[[Category: Buckle, A.M.]]
[[Category: Buckle, A M.]]
[[Category: Burrows, J.M.]]
[[Category: Burrows, J M.]]
[[Category: Burrows, S.R.]]
[[Category: Burrows, S R.]]
[[Category: Clements, C.S.]]
[[Category: Clements, C S.]]
[[Category: Kjer-Nielsen, L.]]
[[Category: Kjer-Nielsen, L.]]
[[Category: Konstenko, L.]]
[[Category: Konstenko, L.]]
[[Category: McCluskey, J.]]
[[Category: McCluskey, J.]]
[[Category: Miles, J.J.]]
[[Category: Miles, J J.]]
[[Category: Purcell, A.W.]]
[[Category: Purcell, A W.]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
[[Category: Silins, S.L.]]
[[Category: Silins, S L.]]
[[Category: Tynan, F.E.]]
[[Category: Tynan, F E.]]
[[Category: Whisstock, J.C.]]
[[Category: Whisstock, J C.]]
[[Category: Wilce, M.C.]]
[[Category: Wilce, M C.]]
[[Category: IOD]]
[[Category: IOD]]
[[Category: bulged epitopes]]
[[Category: bulged epitopes]]
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[[Category: t cell receptor]]
[[Category: t cell receptor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:51:58 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:17 2008''

Revision as of 17:28, 21 February 2008

File:2ak4.gif


2ak4, resolution 2.500Å

Drag the structure with the mouse to rotate

Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide

OverviewOverview

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.

DiseaseDisease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this StructureAbout this Structure

2AK4 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

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