1npu: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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]]' scene=''> | <StructureSection load='1npu' size='340' side='right'caption='[[1npu]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <table><tr><td colspan='2'>[[1npu]] is a 1 chain structure with sequence from [https://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]. 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='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> | </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> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PDCD1_MOUSE PDCD1_MOUSE] Inhibitory cell surface receptor involved in the regulation of T-cell function during immunity and tolerance. Upon ligand binding, inhibits T-cell effector functions in an antigen-specific manner. Possible cell death inducer, in association with other factors (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 16: | Line 19: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1npu ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1npu ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:15030777</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1npu" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Cell death protein 3D structures|Cell death protein 3D structures]] | *[[Cell death protein 3D structures|Cell death protein 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | |||
[[Category: Almo SC]] | [[Category: Almo SC]] | ||
[[Category: Burley SK]] | [[Category: Burley SK]] | ||
