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1npu
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(New page: 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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Revision as of 20:21, 20 November 2007
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CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1
Overview
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 Structure
1NPU is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 22:28:28 2007
Categories: Mus musculus | Single protein | Almo, S.C. | Cao, E. | Chen, L. | Guo, X. | NYSGXRC, New.York.Structural.GenomiX.Research.Consortium. | Nathenson, S.G. | Schwartz, J.C.D. | Zhang, X. | Zhang, Z.Y. | Ig v-type domain | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
