1bqh

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Revision as of 12:43, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1bqh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqh, resolution 2.8Å" /> '''MURINE CD8AA ECTODOMA...)
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File:1bqh.gif


1bqh, resolution 2.8Å

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MURINE CD8AA ECTODOMAIN FRAGMENT IN COMPLEX WITH H-2KB/VSV8

OverviewOverview

The crystal structure of the two immunoglobulin variable-like domains of, the murine CD8alphaalpha homodimer complexed to the class I MHC H-2Kb, molecule at 2.8 A resolution shows that CD8alphaalpha binds to the, protruding MHC alpha3 domain loop in an antibody-like manner. Comparison, of mouse CD8alphaalpha/H-2Kb and human CD8alphaalpha/HLA-A2 complexes, reveals shared as well as species-specific recognition features. In both, species, coreceptor function apparently involves the participation of CD8, dimer in a bidentate attachment to an MHC class I molecule in conjunction, with a T cell receptor without discernable conformational alteration of, the peptide or MHC antigen-presenting platform.

About this StructureAbout this Structure

1BQH is a Protein complex structure of sequences from Mus musculus with NDG and NAG as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-2Kb., Kern PS, Teng MK, Smolyar A, Liu JH, Liu J, Hussey RE, Spoerl R, Chang HC, Reinherz EL, Wang JH, Immunity. 1998 Oct;9(4):519-30. PMID:9806638

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