1b0g

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[[Image:1b0g.jpg|left|200px]]
[[Image:1b0g.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0g OCA], [http://www.ebi.ac.uk/pdbsum/1b0g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0g RCSB]</span>
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'''CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2.1)/BETA 2-MICROGLOBULIN/PEPTIDE P1049 COMPLEX'''
'''CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2.1)/BETA 2-MICROGLOBULIN/PEPTIDE P1049 COMPLEX'''
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==About this Structure==
==About this Structure==
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1B0G is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1A9K. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0G OCA].
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1B0G is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1a9k 1a9k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0G OCA].
==Reference==
==Reference==
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[[Category: Collins, E J.]]
[[Category: Collins, E J.]]
[[Category: Zhao, R.]]
[[Category: Zhao, R.]]
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[[Category: class i histocompatibility antigen (hla-a2 1)/beta 2-microglobulin/peptide p1049 complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:55:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:13 2008''
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Revision as of 07:55, 2 May 2008

Template:STRUCTURE 1b0g

CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2.1)/BETA 2-MICROGLOBULIN/PEPTIDE P1049 COMPLEX


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.

About this Structure

1B0G is a Protein complex structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1a9k. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 10:55:10 2008

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