1eey
From Proteopedia
(New page: 200px<br /> <applet load="1eey" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eey, resolution 2.25Å" /> '''Crystal Structure D...) |
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| - | [[Image:1eey. | + | [[Image:1eey.jpg|left|200px]]<br /><applet load="1eey" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1eey, resolution 2.25Å" /> | caption="1eey, resolution 2.25Å" /> | ||
'''Crystal Structure Determination Of HLA A2 Complexed to Peptide GP2 with the substitution (I2L/V5L/L9V)'''<br /> | '''Crystal Structure Determination Of HLA A2 Complexed to Peptide GP2 with the substitution (I2L/V5L/L9V)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EEY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1EEY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peptide binding]] | [[Category: peptide binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:42:39 2008'' |
Revision as of 13:42, 15 February 2008
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Crystal Structure Determination Of HLA A2 Complexed to Peptide GP2 with the substitution (I2L/V5L/L9V)
Contents |
Overview
An immunogenic peptide (GP2) derived from HER-2/neu binds to HLA-A2.1 very, poorly. Some altered-peptide ligands (APL) of GP2 have increased binding, affinity and generate improved cytotoxic T lymphocyte recognition of, GP2-presenting tumor cells, but most do not. Increases in binding affinity, of single-substitution APL are not additive in double-substitution APL. A, common first assumption about peptide binding to class I major, histocompatibility complex is that each residue binds independently. In, addition, immunologists interested in immunotherapy frequently assume that, anchor substitutions do not affect T cell receptor contact residues., However, the crystal structures of two GP2 APL show that the central, residues change position depending on the identity of the anchor, residue(s). Thus, it is clear that subtle changes in the identity of, anchor residues may have significant effects on the positions of the T, cell receptor contact residues.
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
1EEY is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Class I major histocompatibility complex anchor substitutions alter the conformation of T cell receptor contacts., Sharma AK, Kuhns JJ, Yan S, Friedline RH, Long B, Tisch R, Collins EJ, J Biol Chem. 2001 Jun 15;276(24):21443-9. Epub 2001 Apr 3. PMID:11287414
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