1npu

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Revision as of 23:21, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1npu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npu, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...)
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File:1npu.gif


1npu, resolution 2.00Å

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CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1

OverviewOverview

PD-1, a member of the CD28/CTLA-4/ICOS costimulatory receptor family, delivers negative signals that have profound effects on T and B cell, immunity. The 2.0 A crystal structure of the extracellular domain of, murine PD-1 reveals an Ig V-type topology with overall similarity to the, CTLA-4 monomer; however, there are notable differences in regions relevant, to function. Our structural and biophysical data show that PD-1 is, monomeric both in solution as well as on cell surface, in contrast to, CTLA-4 and other family members that are all disulfide-linked homodimers., Furthermore, our structure-based mutagenesis studies identify the ligand, binding surface of PD-1, which displays significant differences compared, to those present in the other members of the family.

About this StructureAbout this Structure

1NPU is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and functional analysis of the costimulatory receptor programmed death-1., Zhang X, Schwartz JC, Guo X, Bhatia S, Cao E, Lorenz M, Cammer M, Chen L, Zhang ZY, Edidin MA, Nathenson SG, Almo SC, Immunity. 2004 Mar;20(3):337-47. PMID:15030777

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