4z68

From Proteopedia

(Difference between revisions)

Current revision

Hybrid structural analysis of the Arp2/3 regulator Arpin identifies its acidic tail as a primary binding epitope

Structural highlights

4z68 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.859Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARPIN_HUMAN Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence.^[1]

Publication Abstract from PubMed

Arpin is a newly discovered regulator of actin polymerization at the cell leading edge, which steers cell migration by exerting a negative control on the Arp2/3 complex. Arpin proteins have an acidic tail homologous to the acidic motif of the VCA domain of nucleation-promoting factors (NPFs). This tail is predicted to compete with the VCA of NPFs for binding to the Arp2/3 complex, thereby mitigating activation and/or tethering of the complex to sites of actin branching. Here, we investigated the structure of full-length Arpin using synchrotron small-angle X-ray scattering, and of its acidic tail in complex with an ankyrin repeats domain using X-ray crystallography. The data were combined in a hybrid model in which the acidic tail extends from the globular core as a linear peptide and forms a primary epitope that is readily accessible in unbound Arpin and suffices to tether Arpin to interacting proteins with high affinity.

Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope.,Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Perez J, Cherfils J Structure. 2016 Jan 5. pii: S0969-2126(15)00505-5. doi:, 10.1016/j.str.2015.12.001. PMID:26774128^[2]

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

References

↑ Dang I, Gorelik R, Sousa-Blin C, Derivery E, Guérin C, Linkner J, Nemethova M, Dumortier JG, Giger FA, Chipysheva TA, Ermilova VD, Vacher S, Campanacci V, Herrada I, Planson AG, Fetics S, Henriot V, David V, Oguievetskaia K, Lakisic G, Pierre F, Steffen A, Boyreau A, Peyriéras N, Rottner K, Zinn-Justin S, Cherfils J, Bièche I, Alexandrova AY, David NB, Small JV, Faix J, Blanchoin L, Gautreau A. Inhibitory signalling to the Arp2/3 complex steers cell migration. Nature. 2013 Nov 14;503(7475):281-4. PMID:24132237 doi:10.1038/nature12611
↑ Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Perez J, Cherfils J. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure. 2016 Jan 5. pii: S0969-2126(15)00505-5. doi:, 10.1016/j.str.2015.12.001. PMID:26774128 doi:http://dx.doi.org/10.1016/j.str.2015.12.001

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/4z68"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4z68 is ON HOLD  until Paper Publication
+==Hybrid structural analysis of the Arp2/3 regulator Arpin identifies its acidic tail as a primary binding epitope==
+<StructureSection load='4z68' size='340' side='right'caption='[[4z68]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4z68]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z68 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.859&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4z68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z68 OCA], [https://pdbe.org/4z68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z68 RCSB], [https://www.ebi.ac.uk/pdbsum/4z68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z68 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARPIN_HUMAN ARPIN_HUMAN] Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence.<ref>PMID:24132237</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Arpin is a newly discovered regulator of actin polymerization at the cell leading edge, which steers cell migration by exerting a negative control on the Arp2/3 complex. Arpin proteins have an acidic tail homologous to the acidic motif of the VCA domain of nucleation-promoting factors (NPFs). This tail is predicted to compete with the VCA of NPFs for binding to the Arp2/3 complex, thereby mitigating activation and/or tethering of the complex to sites of actin branching. Here, we investigated the structure of full-length Arpin using synchrotron small-angle X-ray scattering, and of its acidic tail in complex with an ankyrin repeats domain using X-ray crystallography. The data were combined in a hybrid model in which the acidic tail extends from the globular core as a linear peptide and forms a primary epitope that is readily accessible in unbound Arpin and suffices to tether Arpin to interacting proteins with high affinity.
-Authors: Fetics, S.K., Campanacci, V., Dang, I., Gautreau, A., Cherfils, J.
+Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope.,Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Perez J, Cherfils J Structure. 2016 Jan 5. pii: S0969-2126(15)00505-5. doi:, 10.1016/j.str.2015.12.001. PMID:26774128<ref>PMID:26774128</ref>
-Description: Structure of an ankyrin repeats domain/peptide complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Campanacci, V]]
+<div class="pdbe-citations 4z68" style="background-color:#fffaf0;"></div>
-[[Category: Fetics, S.K]]
-[[Category: Cherfils, J]]
+==See Also==
-[[Category: Gautreau, A]]
+*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
-[[Category: Dang, I]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Campanacci V]]
+[[Category: Cherfils J]]
+[[Category: Dang I]]
+[[Category: Fetics SK]]
+[[Category: Gautreau A]]

4z68

From Proteopedia

Current revision

Hybrid structural analysis of the Arp2/3 regulator Arpin identifies its acidic tail as a primary binding epitope

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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