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3bp5

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Revision as of 08:07, 25 October 2017

Crystal structure of the mouse PD-1 and PD-L2 complex

Structural highlights

3bp5 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3bp6
Gene:	Pdcd1, Pd1 (Mus musculus), Pdcd1lg2, B7dc, Btdc, Cd273, Pdl2 (Mus musculus)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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). [PD1L2_MOUSE] Involved in the costimulatory signal essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.^[1] ^[2] ^[3]

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 PubMed

Programmed death-1 (PD-1) is a member of the CD28/B7 superfamily that delivers negative signals upon interaction with its two ligands, PD-L1 or PD-L2. The high-resolution crystal structure of the complex formed by the complete ectodomains of murine PD-1 and PD-L2 revealed a 1:1 receptor:ligand stoichiometry and displayed a binding interface and overall molecular organization distinct from that observed in the CTLA-4/B7 inhibitory complexes. Furthermore, our structure also provides insights into the association between PD-1 and PD-L1 and highlights differences in the interfaces formed by the two PD-1 ligands (PD-Ls) Mutagenesis studies confirmed the details of the proposed PD-1/PD-L binding interfaces and allowed for the design of a mutant PD-1 receptor with enhanced affinity. These studies define spatial and organizational constraints that control the localization and signaling of PD-1/PD-L complexes within the immunological synapse and provide a basis for manipulating the PD-1 pathways for immunotherapy.

Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2.,Lazar-Molnar E, Yan Q, Cao E, Ramagopal U, Nathenson SG, Almo SC Proc Natl Acad Sci U S A. 2008 Jul 29;105(30):10483-8. Epub 2008 Jul 18. PMID:18641123^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tseng SY, Otsuji M, Gorski K, Huang X, Slansky JE, Pai SI, Shalabi A, Shin T, Pardoll DM, Tsuchiya H. B7-DC, a new dendritic cell molecule with potent costimulatory properties for T cells. J Exp Med. 2001 Apr 2;193(7):839-46. PMID:11283156
↑ Latchman Y, Wood CR, Chernova T, Chaudhary D, Borde M, Chernova I, Iwai Y, Long AJ, Brown JA, Nunes R, Greenfield EA, Bourque K, Boussiotis VA, Carter LL, Carreno BM, Malenkovich N, Nishimura H, Okazaki T, Honjo T, Sharpe AH, Freeman GJ. PD-L2 is a second ligand for PD-1 and inhibits T cell activation. Nat Immunol. 2001 Mar;2(3):261-8. PMID:11224527 doi:http://dx.doi.org/10.1038/85330
↑ Wang S, Bajorath J, Flies DB, Dong H, Honjo T, Chen L. Molecular modeling and functional mapping of B7-H1 and B7-DC uncouple costimulatory function from PD-1 interaction. J Exp Med. 2003 May 5;197(9):1083-91. Epub 2003 Apr 28. PMID:12719480 doi:http://dx.doi.org/10.1084/jem.20021752
↑ Lazar-Molnar E, Yan Q, Cao E, Ramagopal U, Nathenson SG, Almo SC. Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2. Proc Natl Acad Sci U S A. 2008 Jul 29;105(30):10483-8. Epub 2008 Jul 18. PMID:18641123

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bp5"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the mouse PD-1 and PD-L2 complex==
 <StructureSection load='3bp5' size='340' side='right' caption='[[3bp5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bp6|3bp6]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pdcd1, Pd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), Pdcd1lg2, B7dc, Btdc, Cd273, Pdl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bp5 OCA], [http://pdbe.org/3bp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bp5 RCSB], [http://www.ebi.ac.uk/pdbsum/3bp5 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bp5 OCA], [http://pdbe.org/3bp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bp5 RCSB], [http://www.ebi.ac.uk/pdbsum/3bp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bp5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 3bp5" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cell death protein|Cell death protein]]
 == References ==
 <references/>

3bp5

From Proteopedia

Revision as of 08:07, 25 October 2017

Crystal structure of the mouse PD-1 and PD-L2 complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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