1sjh

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[[Image:1sjh.gif|left|200px]]<br /><applet load="1sjh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sjh.gif|left|200px]]
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caption="1sjh, resolution 2.25&Aring;" />
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'''HLA-DR1 complexed with a 13 residue HIV capsid peptide'''<br />
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{{Structure
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|PDB= 1sjh |SIZE=350|CAPTION= <scene name='initialview01'>1sjh</scene>, resolution 2.25&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= HLA-DRA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), HLA-DRB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), ENTC3, SAV2009, SA1817 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
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}}
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'''HLA-DR1 complexed with a 13 residue HIV capsid peptide'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1SJH is a [[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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15331779 15331779]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15331779 15331779]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: superantigen]]
[[Category: superantigen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:05:45 2008''

Revision as of 12:05, 20 March 2008


PDB ID 1sjh

Drag the structure with the mouse to rotate
, resolution 2.25Å
Gene: HLA-DRA (Homo sapiens), HLA-DRB1 (Homo sapiens), ENTC3, SAV2009, SA1817 (Staphylococcus aureus)
Coordinates: save as pdb, mmCIF, xml



HLA-DR1 complexed with a 13 residue HIV capsid peptide


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.

About this Structure

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

Reference

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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