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==CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1== | ==CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1== | ||
<StructureSection load='1npu' size='340' side='right' caption='[[1npu]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1npu' size='340' side='right'caption='[[1npu]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NPU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1npu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npu OCA], [https://pdbe.org/1npu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1npu RCSB], [https://www.ebi.ac.uk/pdbsum/1npu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1npu ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1npu TOPSAN]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/np/1npu_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/np/1npu_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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==See Also== | ==See Also== | ||
*[[Cell death protein|Cell death protein]] | *[[Cell death protein 3D structures|Cell death protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Almo | [[Category: Almo SC]] | ||
[[Category: Burley | [[Category: Burley SK]] | ||
[[Category: Cao | [[Category: Cao E]] | ||
[[Category: Chen | [[Category: Chen L]] | ||
[[Category: Guo | [[Category: Guo X]] | ||
[[Category: Nathenson SG]] | |||
[[Category: Nathenson | [[Category: Schwartz J-CD]] | ||
[[Category: Schwartz | [[Category: Zhang X]] | ||
[[Category: Zhang | [[Category: Zhang Z-Y]] | ||
[[Category: Zhang | |||
Latest revision as of 10:05, 30 October 2024
CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPD-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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