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5l5g

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Plexin A2 full extracellular region, domains 1 to 8 modeled, data to 10 angstrom

Structural highlights

5l5g is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 10Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLXA2_MOUSE Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Class A plexins (PlxnAs) act as semaphorin receptors and control diverse aspects of nervous system development and plasticity, ranging from axon guidance and neuron migration to synaptic organization. PlxnA signaling requires cytoplasmic domain dimerization, but extracellular regulation and activation mechanisms remain unclear. Here we present crystal structures of PlxnA (PlxnA1, PlxnA2, and PlxnA4) full ectodomains. Domains 1-9 form a ring-like conformation from which the C-terminal domain 10 points away. All our PlxnA ectodomain structures show autoinhibitory, intermolecular "head-to-stalk" (domain 1 to domain 4-5) interactions, which are confirmed by biophysical assays, live cell fluorescence microscopy, and cell-based and neuronal growth cone collapse assays. This work reveals a 2-fold role of the PlxnA ectodomains: imposing a pre-signaling autoinhibitory separation for the cytoplasmic domains via intermolecular head-to-stalk interactions and supporting dimerization-based PlxnA activation upon ligand binding. More generally, our data identify a novel molecular mechanism for preventing premature activation of axon guidance receptors.

Structural Basis for Plexin Activation and Regulation.,Kong Y, Janssen BJ, Malinauskas T, Vangoor VR, Coles CH, Kaufmann R, Ni T, Gilbert RJ, Padilla-Parra S, Pasterkamp RJ, Jones EY Neuron. 2016 Jul 5. pii: S0896-6273(16)30295-1. doi:, 10.1016/j.neuron.2016.06.018. PMID:27397516^[4]

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

References

↑ Takahashi T, Fournier A, Nakamura F, Wang LH, Murakami Y, Kalb RG, Fujisawa H, Strittmatter SM. Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors. Cell. 1999 Oct 1;99(1):59-69. PMID:10520994
↑ Rohm B, Ottemeyer A, Lohrum M, Puschel AW. Plexin/neuropilin complexes mediate repulsion by the axonal guidance signal semaphorin 3A. Mech Dev. 2000 May;93(1-2):95-104. PMID:10781943
↑ Janssen BJ, Robinson RA, Perez-Branguli F, Bell CH, Mitchell KJ, Siebold C, Jones EY. Structural basis of semaphorin-plexin signalling. Nature. 2010 Sep 26. PMID:20877282 doi:10.1038/nature09468
↑ Kong Y, Janssen BJ, Malinauskas T, Vangoor VR, Coles CH, Kaufmann R, Ni T, Gilbert RJ, Padilla-Parra S, Pasterkamp RJ, Jones EY. Structural Basis for Plexin Activation and Regulation. Neuron. 2016 Jul 5. pii: S0896-6273(16)30295-1. doi:, 10.1016/j.neuron.2016.06.018. PMID:27397516 doi:http://dx.doi.org/10.1016/j.neuron.2016.06.018

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/5l5g"

@@ Line 1: / Line 1: @@
 ==Plexin A2 full extracellular region, domains 1 to 8 modeled, data to 10 angstrom==
-<StructureSection load='5l5g' size='340' side='right' caption='[[5l5g]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
+<StructureSection load='5l5g' size='340' side='right'caption='[[5l5g]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5l5g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L5G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L5G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5l5g]] is a 4 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=5L5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L5G FirstGlance]. <br>
-</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=5l5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l5g OCA], [http://pdbe.org/5l5g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l5g RCSB], [http://www.ebi.ac.uk/pdbsum/5l5g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l5g ProSAT]</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]] 10&#8491;</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=5l5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l5g OCA], [https://pdbe.org/5l5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l5g RCSB], [https://www.ebi.ac.uk/pdbsum/5l5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l5g ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PLXA2_MOUSE PLXA2_MOUSE]] Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.<ref>PMID:10520994</ref> <ref>PMID:10781943</ref> <ref>PMID:20877282</ref>
+[https://www.uniprot.org/uniprot/PLXA2_MOUSE PLXA2_MOUSE] Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.<ref>PMID:10520994</ref> <ref>PMID:10781943</ref> <ref>PMID:20877282</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5l5g" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Plexin 3D structures|Plexin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Coles, C H]]
+[[Category: Large Structures]]
-[[Category: Gilbert, R J.C]]
+[[Category: Mus musculus]]
-[[Category: Janssen, B J.C]]
+[[Category: Coles CH]]
-[[Category: Jones, E Y]]
+[[Category: Gilbert RJC]]
-[[Category: Kaufmann, R]]
+[[Category: Janssen BJC]]
-[[Category: Kong, Y]]
+[[Category: Jones EY]]
-[[Category: Malinauskas, T]]
+[[Category: Kaufmann R]]
-[[Category: Ni, T]]
+[[Category: Kong Y]]
-[[Category: Padilla-Parra, S]]
+[[Category: Malinauskas T]]
-[[Category: Pasterkamp, R J]]
+[[Category: Ni T]]
-[[Category: Vangoor, V R]]
+[[Category: Padilla-Parra S]]
-[[Category: Axon guidance]]
+[[Category: Pasterkamp RJ]]
-[[Category: Receptor]]
+[[Category: Vangoor VR]]
-[[Category: Signaling]]
-[[Category: Signaling protein]]

5l5g

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Current revision

Plexin A2 full extracellular region, domains 1 to 8 modeled, data to 10 angstrom

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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