1bz9: Difference between revisions

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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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1bz9.gif|left|200px]]<br /><applet load="1bz9" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1bz9, resolution 2.8&Aring;" />
caption="1bz9, resolution 2.8&Aring;" />
'''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, 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.
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 superseeds the now removed PDB entry 1A9D. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BZ9 OCA].  
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.J.]]
[[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

File:1bz9.gif


1bz9, resolution 2.8Å

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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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