4zi2

From Proteopedia

(Difference between revisions)

Current revision

BART-like domain of BARTL1/CCDC104 in complex with Arl3FL bound to GppNHp in P21 21 21

Structural highlights

4zi2 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 2.2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARL3_MOUSE Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium (By similarity). Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms.^[1] ^[2]

Publication Abstract from PubMed

Cilia are small antenna-like cellular protrusions critical for many developmental signaling pathways. The ciliary protein Arl3 has been shown to act as a specific release factor for myristoylated and farnesylated ciliary cargo molecules by binding to the effectors Unc119 and PDE6delta. Here we describe a newly identified Arl3 binding partner, CCDC104/CFAP36. Biochemical and structural analyses reveal that the protein contains a BART-like domain and is called BARTL1. It recognizes an LLxILxxL motif at the N-terminal amphipathic helix of Arl3, which is crucial for the interaction with the BART-like domain but also for the ciliary localization of Arl3 itself. These results seem to suggest a ciliary role of BARTL1, and possibly link it to the Arl3 transport network. We thus speculate on a regulatory mechanism whereby BARTL1 aids the presentation of active Arl3 to its GTPase-activating protein RP2 or hinders Arl3 membrane binding in the area of the transition zone.

The Interaction of CCDC104/BARTL1 with Arl3 and Implications for Ciliary Function.,Lokaj M, Kosling SK, Koerner C, Lange SM, van Beersum SE, van Reeuwijk J, Roepman R, Horn N, Ueffing M, Boldt K, Wittinghofer A Structure. 2015 Nov 3;23(11):2122-32. doi: 10.1016/j.str.2015.08.016. Epub 2015, Oct 9. PMID:26455799^[3]

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

References

↑ Hanzal-Bayer M, Linari M, Wittinghofer A. Properties of the interaction of Arf-like protein 2 with PDEdelta. J Mol Biol. 2005 Jul 29;350(5):1074-82. PMID:15979089 doi:10.1016/j.jmb.2005.05.036
↑ Veltel S, Gasper R, Eisenacher E, Wittinghofer A. The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3. Nat Struct Mol Biol. 2008 Apr;15(4):373-80. Epub 2008 Mar 23. PMID:18376416 doi:nsmb.1396
↑ Lokaj M, Kosling SK, Koerner C, Lange SM, van Beersum SE, van Reeuwijk J, Roepman R, Horn N, Ueffing M, Boldt K, Wittinghofer A. The Interaction of CCDC104/BARTL1 with Arl3 and Implications for Ciliary Function. Structure. 2015 Nov 3;23(11):2122-32. doi: 10.1016/j.str.2015.08.016. Epub 2015, Oct 9. PMID:26455799 doi:http://dx.doi.org/10.1016/j.str.2015.08.016

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4zi2"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4zi2]] 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=4ZI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZI2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4zi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zi2 OCA], [https://pdbe.org/4zi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zi2 RCSB], [https://www.ebi.ac.uk/pdbsum/4zi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zi2 ProSAT]</span></td></tr>
 </table>

4zi2

From Proteopedia

Current revision

BART-like domain of BARTL1/CCDC104 in complex with Arl3FL bound to GppNHp in P21 21 21

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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