1sjh: Difference between revisions

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[[Image:1sjh.gif|left|200px]]<br />
[[Image:1sjh.gif|left|200px]]<br /><applet load="1sjh" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1sjh" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1sjh, resolution 2.25&Aring;" />
caption="1sjh, resolution 2.25&Aring;" />
'''HLA-DR1 complexed with a 13 residue HIV capsid peptide'''<br />
'''HLA-DR1 complexed with a 13 residue HIV capsid peptide'''<br />


==Overview==
==Overview==
T cells generally recognize peptide antigens bound to MHC proteins through, contacts with residues found within or immediately flanking the seven- to, nine-residue sequence accommodated in the MHC peptide-binding groove., However, some T cells require peptide residues outside this region for, activation, the structural basis for which is unknown. Here, we have, investigated a HIV Gag-specific T cell clone that requires an unusually, long peptide antigen for activation. The crystal structure of a minimally, antigenic 16-mer bound to HLA-DR1 shows that the peptide C-terminal region, bends sharply into a hairpin turn as it exits the binding site, orienting, peptide residues outside the MHC-binding region in position to interact, with a T cell receptor. Peptide truncation and substitution studies show, that both the hairpin turn and the extreme C-terminal residues are, required for T cell activation. These results demonstrate a previously, unrecognized mode of MHC-peptide-T cell receptor interaction.
T cells generally recognize peptide antigens bound to MHC proteins through contacts with residues found within or immediately flanking the seven- to nine-residue sequence accommodated in the MHC peptide-binding groove. However, some T cells require peptide residues outside this region for activation, the structural basis for which is unknown. Here, we have investigated a HIV Gag-specific T cell clone that requires an unusually long peptide antigen for activation. The crystal structure of a minimally antigenic 16-mer bound to HLA-DR1 shows that the peptide C-terminal region bends sharply into a hairpin turn as it exits the binding site, orienting peptide residues outside the MHC-binding region in position to interact with a T cell receptor. Peptide truncation and substitution studies show that both the hairpin turn and the extreme C-terminal residues are required for T cell activation. These results demonstrate a previously unrecognized mode of MHC-peptide-T cell receptor interaction.


==About this Structure==
==About this Structure==
1SJH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SJH OCA].  
1SJH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJH OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Norris, P.J.]]
[[Category: Norris, P J.]]
[[Category: Stern, L.J.]]
[[Category: Stern, L J.]]
[[Category: Strug, I.]]
[[Category: Strug, I.]]
[[Category: Walker, B.D.]]
[[Category: Walker, B D.]]
[[Category: Zavala-Ruiz, Z.]]
[[Category: Zavala-Ruiz, Z.]]
[[Category: antigen]]
[[Category: antigen]]
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[[Category: superantigen]]
[[Category: superantigen]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:14:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:07 2008''

Revision as of 16:02, 21 February 2008

File:1sjh.gif


1sjh, resolution 2.25Å

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HLA-DR1 complexed with a 13 residue HIV capsid peptide

OverviewOverview

T cells generally recognize peptide antigens bound to MHC proteins through contacts with residues found within or immediately flanking the seven- to nine-residue sequence accommodated in the MHC peptide-binding groove. However, some T cells require peptide residues outside this region for activation, the structural basis for which is unknown. Here, we have investigated a HIV Gag-specific T cell clone that requires an unusually long peptide antigen for activation. The crystal structure of a minimally antigenic 16-mer bound to HLA-DR1 shows that the peptide C-terminal region bends sharply into a hairpin turn as it exits the binding site, orienting peptide residues outside the MHC-binding region in position to interact with a T cell receptor. Peptide truncation and substitution studies show that both the hairpin turn and the extreme C-terminal residues are required for T cell activation. These results demonstrate a previously unrecognized mode of MHC-peptide-T cell receptor interaction.

About this StructureAbout this Structure

1SJH is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition., Zavala-Ruiz Z, Strug I, Walker BD, Norris PJ, Stern LJ, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13279-84. Epub 2004 Aug 26. PMID:15331779

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