1bz9: Difference between revisions
New page: left|200px<br /><applet load="1bz9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bz9, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1bz9.gif|left|200px]]<br /><applet load="1bz9" size=" | [[Image:1bz9.gif|left|200px]]<br /><applet load="1bz9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1bz9, resolution 2.8Å" /> | caption="1bz9, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF MURINE CLASS I MHC H2-DB COMPLEXED WITH A SYNTHETIC PEPTIDE P1027'''<br /> | '''CRYSTAL STRUCTURE OF MURINE CLASS I MHC H2-DB COMPLEXED WITH A SYNTHETIC PEPTIDE P1027'''<br /> | ||
==Overview== | ==Overview== | ||
The T cell receptor (TCR), from a xeno-reactive murine cytotoxic T | The T cell receptor (TCR), from a xeno-reactive murine cytotoxic T lymphocyte clone AHIII12.2, recognizes murine H-2Db complexed with peptide p1027 (FAPGVFPYM), as well as human HLA-A2.1 complexed with peptide p1049 (ALWGFFPVL). A commonly proposed model (the molecular mimicry model) used to explain TCR cross-reactivity suggests that the molecular surfaces of the recognized complexes are similar in shape, charge, or both, in spite of the primary sequence differences. To examine the mechanism of xeno-reactivity of AHIII12.2, we have determined the crystal structures of A2/p1049 and Db/p1027 to 2.5 A and 2.8 A resolution, respectively. The crystal structures show that the TCR footprint regions of the two class I complexes are significantly different in shape and charge. We propose that rather than simple molecular mimicry, unpredictable arrays of common and differential contacts on the two class I complexes are used for their recognition by the same TCR. | ||
==About this Structure== | ==About this Structure== | ||
1BZ9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure | 1BZ9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry 1A9D. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BZ9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Collins, E | [[Category: Collins, E J.]] | ||
[[Category: Zhao, R.]] | [[Category: Zhao, R.]] | ||
[[Category: murine class i mhc/peptide complex]] | [[Category: murine class i mhc/peptide complex]] | ||
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Revision as of 13:00, 21 February 2008
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CRYSTAL STRUCTURE OF MURINE CLASS I MHC H2-DB COMPLEXED WITH A SYNTHETIC PEPTIDE P1027
OverviewOverview
The T cell receptor (TCR), from a xeno-reactive murine cytotoxic T lymphocyte clone AHIII12.2, recognizes murine H-2Db complexed with peptide p1027 (FAPGVFPYM), as well as human HLA-A2.1 complexed with peptide p1049 (ALWGFFPVL). A commonly proposed model (the molecular mimicry model) used to explain TCR cross-reactivity suggests that the molecular surfaces of the recognized complexes are similar in shape, charge, or both, in spite of the primary sequence differences. To examine the mechanism of xeno-reactivity of AHIII12.2, we have determined the crystal structures of A2/p1049 and Db/p1027 to 2.5 A and 2.8 A resolution, respectively. The crystal structures show that the TCR footprint regions of the two class I complexes are significantly different in shape and charge. We propose that rather than simple molecular mimicry, unpredictable arrays of common and differential contacts on the two class I complexes are used for their recognition by the same TCR.
About this StructureAbout this Structure
1BZ9 is a Protein complex structure of sequences from Mus musculus. This structure supersedes the now removed PDB entry 1A9D. Full crystallographic information is available from OCA.
ReferenceReference
Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry., Zhao R, Loftus DJ, Appella E, Collins EJ, J Exp Med. 1999 Jan 18;189(2):359-70. PMID:9892618
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