1npu: Difference between revisions

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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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[[Image:1npu.gif|left|200px]]<br /><applet load="1npu" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1npu.gif|left|200px]]<br /><applet load="1npu" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1npu, resolution 2.00&Aring;" />
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'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1'''<br />
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1'''<br />


==Overview==
==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.
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==
==About this Structure==
1NPU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NPU OCA].  
1NPU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPU OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Almo, S.C.]]
[[Category: Almo, S C.]]
[[Category: Cao, E.]]
[[Category: Cao, E.]]
[[Category: Chen, L.]]
[[Category: Chen, L.]]
[[Category: Guo, X.]]
[[Category: Guo, X.]]
[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Nathenson, S.G.]]
[[Category: Nathenson, S G.]]
[[Category: Schwartz, J.C.D.]]
[[Category: Schwartz, J C.D.]]
[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
[[Category: Zhang, Z.Y.]]
[[Category: Zhang, Z Y.]]
[[Category: ig v-type domain]]
[[Category: ig v-type domain]]
[[Category: new york structural genomix research consortium]]
[[Category: new york structural genomix research consortium]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:28:28 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:41 2008''

Revision as of 15:08, 21 February 2008

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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