1x7q
From Proteopedia
(New page: 200px<br /> <applet load="1x7q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x7q, resolution 1.45Å" /> '''Crystal structure o...) |
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| - | [[Image:1x7q.gif|left|200px]]<br /> | + | [[Image:1x7q.gif|left|200px]]<br /><applet load="1x7q" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1x7q" size=" | + | |
caption="1x7q, resolution 1.45Å" /> | caption="1x7q, resolution 1.45Å" /> | ||
'''Crystal structure of HLA-A*1101 with sars nucleocapsid peptide'''<br /> | '''Crystal structure of HLA-A*1101 with sars nucleocapsid peptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the human MHC-I molecule HLA-A*1101 in complex with a | + | The structure of the human MHC-I molecule HLA-A*1101 in complex with a nonameric peptide (KTFPPTEPK) has been determined by X-ray crystallography to 1.45 A resolution. The peptide is derived from the SARS-CoV nucleocapsid protein positions 362-370 (SNP362-370). It is conserved in all known isolates of SARS-CoV and has been verified by in vitro peptide-binding studies to be a good to intermediate binder to HLA-A*0301 and HLA-A*1101, with IC50 values of 70 and 186 nM, respectively [Sylvester-Hvid et al. (2004), Tissue Antigens, 63, 395-400]. In terms of the residues lining the peptide-binding groove, the HLA-A*1101-SNP362-370 complex is very similar to other known structures of HLA-A*1101 and HLA-A*6801. The SNP362-370 peptide is held in place by 17 hydrogen bonds to the alpha-chain residues and by nine water molecules which are also tightly bound in the peptide-binding groove. Thr6 of the peptide (Thr6p) does not make efficient use of the middle (E) pocket. For vaccine development, there seems to be a potential for optimization targeted at this position. All residues except Thr2p and Lys9p are accessible for T-cell recognition. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1X7Q 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 SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1X7Q 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=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Buus, S.]] | [[Category: Buus, S.]] | ||
[[Category: Gajhede, M.]] | [[Category: Gajhede, M.]] | ||
| - | [[Category: Kastrup, J | + | [[Category: Kastrup, J S.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: sars]] | [[Category: sars]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:51:51 2008'' |
Revision as of 13:51, 21 February 2008
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Crystal structure of HLA-A*1101 with sars nucleocapsid peptide
Contents |
Overview
The structure of the human MHC-I molecule HLA-A*1101 in complex with a nonameric peptide (KTFPPTEPK) has been determined by X-ray crystallography to 1.45 A resolution. The peptide is derived from the SARS-CoV nucleocapsid protein positions 362-370 (SNP362-370). It is conserved in all known isolates of SARS-CoV and has been verified by in vitro peptide-binding studies to be a good to intermediate binder to HLA-A*0301 and HLA-A*1101, with IC50 values of 70 and 186 nM, respectively [Sylvester-Hvid et al. (2004), Tissue Antigens, 63, 395-400]. In terms of the residues lining the peptide-binding groove, the HLA-A*1101-SNP362-370 complex is very similar to other known structures of HLA-A*1101 and HLA-A*6801. The SNP362-370 peptide is held in place by 17 hydrogen bonds to the alpha-chain residues and by nine water molecules which are also tightly bound in the peptide-binding groove. Thr6 of the peptide (Thr6p) does not make efficient use of the middle (E) pocket. For vaccine development, there seems to be a potential for optimization targeted at this position. All residues except Thr2p and Lys9p are accessible for T-cell recognition.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]
About this Structure
1X7Q is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid peptide., Blicher T, Kastrup JS, Buus S, Gajhede M, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1031-40. Epub 2005, Jul 20. PMID:16041067
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