2clr: Difference between revisions
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[[Image:2clr.gif|left|200px]] | [[Image:2clr.gif|left|200px]] | ||
'''THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE''' | {{Structure | ||
|PDB= 2clr |SIZE=350|CAPTION= <scene name='initialview01'>2clr</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= BETA-2-MICROGLOBULIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CLR is a [ | 2CLR is a [[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=2CLR OCA]. | ||
==Reference== | ==Reference== | ||
Three-dimensional structure of a peptide extending from one end of a class I MHC binding site., Collins EJ, Garboczi DN, Wiley DC, Nature. 1994 Oct 13;371(6498):626-9. PMID:[http:// | Three-dimensional structure of a peptide extending from one end of a class I MHC binding site., Collins EJ, Garboczi DN, Wiley DC, Nature. 1994 Oct 13;371(6498):626-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7935798 7935798] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:57 2008'' | ||
Revision as of 17:17, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Gene: | BETA-2-MICROGLOBULIN (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE
OverviewOverview
Class I major histocompatibility complex (MHC) molecules present peptides to CD8+ T cells for immunological surveillance (reviewed in ref. 1). The structures of complexes of class I MHC molecules with octamer, nonamer and decamer peptides determined until now show a common binding mode, with both peptide termini bound in conserved pockets at the ends of the peptide binding site. Length variations were accommodated by the peptide bulging or zig-zagging in the middle. Here we describe the structure of a decamer peptide which binds with the carboxy-terminal residue positioned outside the peptide binding site. Several protein side chains have rearranged to allow the peptide to exit. The structure suggests that even longer peptides could bind. The energetic effect of the altered mode of binding has been assessed by measuring the stability of the complex to thermal denaturation. Peptides bound in this novel manner are stable at physiological temperature, raising questions about their role in T-cell recognition and their production by proteolytic processing.
DiseaseDisease
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 StructureAbout this Structure
2CLR is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of a peptide extending from one end of a class I MHC binding site., Collins EJ, Garboczi DN, Wiley DC, Nature. 1994 Oct 13;371(6498):626-9. PMID:7935798
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