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4yfd

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Revision as of 01:58, 10 March 2017

Crystal structure PTP delta Ig1-Fn2 in complex with IL-1RAcP

Structural highlights

4yfd is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4yfc, 4yfe, 4yfg
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IL1AP_MOUSE] Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Secreted forms (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors.[UniProtKB:Q9NPH3]^[1]

Publication Abstract from PubMed

Synapse formation is triggered through trans-synaptic interaction between pairs of pre- and postsynaptic adhesion molecules, the specificity of which depends on splice inserts known as 'splice-insert signaling codes'. Receptor protein tyrosine phosphatase delta (PTPdelta) can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to interleukin-1 receptor accessory protein (IL-1RAcP) and IL-1RAcP-like-1 (IL1RAPL1) in a splicing-dependent manner. Here, we report crystal structures of PTPdelta in complex with IL1RAPL1 and IL-1RAcP. The first immunoglobulin-like (Ig) domain of IL1RAPL1 directly recognizes the first splice insert, which is critical for binding to IL1RAPL1. The second splice insert functions as an adjustable linker that positions the Ig2 and Ig3 domains of PTPdelta for simultaneously interacting with the Ig1 domain of IL1RAPL1 or IL-1RAcP. We further identified the IL1RAPL1-specific interaction, which appears coupled to the first-splice-insert-mediated interaction. Our results thus reveal the decoding mechanism of splice-insert signaling codes for synaptic differentiation induced by trans-synaptic adhesion between PTPdelta and IL1RAPL1/IL-1RAcP.

Mechanisms of splicing-dependent trans-synaptic adhesion by PTPdelta-IL1RAPL1/IL-1RAcP for synaptic differentiation.,Yamagata A, Yoshida T, Sato Y, Goto-Ito S, Uemura T, Maeda A, Shiroshima T, Iwasawa-Okamoto S, Mori H, Mishina M, Fukai S Nat Commun. 2015 Apr 24;6:6926. doi: 10.1038/ncomms7926. PMID:25908590^[2]

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

References

↑ Towne JE, Renshaw BR, Douangpanya J, Lipsky BP, Shen M, Gabel CA, Sims JE. Interleukin-36 (IL-36) ligands require processing for full agonist (IL-36alpha, IL-36beta, and IL-36gamma) or antagonist (IL-36Ra) activity. J Biol Chem. 2011 Dec 9;286(49):42594-602. doi: 10.1074/jbc.M111.267922. Epub, 2011 Sep 29. PMID:21965679 doi:http://dx.doi.org/10.1074/jbc.M111.267922
↑ Yamagata A, Yoshida T, Sato Y, Goto-Ito S, Uemura T, Maeda A, Shiroshima T, Iwasawa-Okamoto S, Mori H, Mishina M, Fukai S. Mechanisms of splicing-dependent trans-synaptic adhesion by PTPdelta-IL1RAPL1/IL-1RAcP for synaptic differentiation. Nat Commun. 2015 Apr 24;6:6926. doi: 10.1038/ncomms7926. PMID:25908590 doi:http://dx.doi.org/10.1038/ncomms7926

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4yfd"

@@ Line 1: / Line 1: @@
 ==Crystal structure PTP delta Ig1-Fn2 in complex with IL-1RAcP==
 <StructureSection load='4yfd' size='340' side='right' caption='[[4yfd]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yfc|4yfc]], [[4yfe|4yfe]], [[4yfg|4yfg]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=4yfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yfd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yfd RCSB], [http://www.ebi.ac.uk/pdbsum/4yfd 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=4yfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yfd OCA], [http://pdbe.org/4yfd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yfd RCSB], [http://www.ebi.ac.uk/pdbsum/4yfd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yfd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4yfd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tyrosine phosphatase|Tyrosine phosphatase]]
 == References ==
 <references/>

4yfd

From Proteopedia

Revision as of 01:58, 10 March 2017

Crystal structure PTP delta Ig1-Fn2 in complex with IL-1RAcP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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