This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4mt6

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 01:56, 5 August 2016

Crystal structure of closed inactive collybistin

Structural highlights

4mt6 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4mt7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ARHG9_RAT] Acts as guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The formation of neuronal synapses and the dynamic regulation of their efficacy depend on the assembly of the postsynaptic neurotransmitter receptor apparatus. Receptor recruitment to inhibitory GABAergic and glycinergic synapses is controlled by the scaffold protein gephyrin and the adaptor protein collybistin. We derived new insights into the structure of collybistin and used these to design biochemical, cell biological, and genetic analyses of collybistin function. Our data define a collybistin-based protein interaction network that controls the gephyrin content of inhibitory postsynapses. Within this network, collybistin can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin to plasma membrane phosphoinositides. This function of collybistin is regulated by binding of the adhesion protein neuroligin-2, which stabilizes the open/active conformation of collybistin at the postsynaptic plasma membrane by competing with an intramolecular interaction in collybistin that favors the closed/inactive conformation. By linking trans-synaptic neuroligin-dependent adhesion and phosphoinositide signaling with gephyrin recruitment, the collybistin-based regulatory switch mechanism represents an integrating regulatory node in the formation and function of inhibitory postsynapses.

A conformational switch in collybistin determines the differentiation of inhibitory postsynapses.,Soykan T, Schneeberger D, Tria G, Buechner C, Bader N, Svergun D, Tessmer I, Poulopoulos A, Papadopoulos T, Varoqueaux F, Schindelin H, Brose N EMBO J. 2014 Jul 30. pii: e201488143. PMID:25082542^[4]

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

References

↑ Kins S, Betz H, Kirsch J. Collybistin, a newly identified brain-specific GEF, induces submembrane clustering of gephyrin. Nat Neurosci. 2000 Jan;3(1):22-9. PMID:10607391 doi:http://dx.doi.org/10.1038/71096
↑ Grosskreutz Y, Hermann A, Kins S, Fuhrmann JC, Betz H, Kneussel M. Identification of a gephyrin-binding motif in the GDP/GTP exchange factor collybistin. Biol Chem. 2001 Oct;382(10):1455-62. PMID:11727829 doi:http://dx.doi.org/10.1515/BC.2001.179
↑ Harvey K, Duguid IC, Alldred MJ, Beatty SE, Ward H, Keep NH, Lingenfelter SE, Pearce BR, Lundgren J, Owen MJ, Smart TG, Luscher B, Rees MI, Harvey RJ. The GDP-GTP exchange factor collybistin: an essential determinant of neuronal gephyrin clustering. J Neurosci. 2004 Jun 23;24(25):5816-26. PMID:15215304 doi:10.1523/JNEUROSCI.1184-04.2004
↑ Soykan T, Schneeberger D, Tria G, Buechner C, Bader N, Svergun D, Tessmer I, Poulopoulos A, Papadopoulos T, Varoqueaux F, Schindelin H, Brose N. A conformational switch in collybistin determines the differentiation of inhibitory postsynapses. EMBO J. 2014 Jul 30. pii: e201488143. PMID:25082542 doi:http://dx.doi.org/10.15252/embj.201488143

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/4mt6"

Categories: Schindelin, H | Schneeberger, D | Closed conformation | Protein binding

@@ Line 1: / Line 1: @@
 ==Crystal structure of closed inactive collybistin==
 <StructureSection load='4mt6' size='340' side='right' caption='[[4mt6]], [[Resolution|resolution]] 5.50&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4mt6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MT6 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mt7|4mt7]]</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=4mt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mt6 RCSB], [http://www.ebi.ac.uk/pdbsum/4mt6 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=4mt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mt6 OCA], [http://pdbe.org/4mt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mt6 RCSB], [http://www.ebi.ac.uk/pdbsum/4mt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mt6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4mt6" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Rho guanine nucleotide exchange factor|Rho guanine nucleotide exchange factor]]
 == References ==
 <references/>

4mt6

From Proteopedia

Revision as of 01:56, 5 August 2016

Crystal structure of closed inactive collybistin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox