4rml

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the Olfactomedin domain of latrophilin 3 in C2221 crystal form

Structural highlights

4rml is a 1 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 1.601Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AGRL3_MOUSE Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25728924, PubMed:26235031). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Latrophilins (LPHNs) are adhesion-like G-protein-coupled receptors implicated in attention-deficit/hyperactivity disorder. Recently, LPHN3 was found to regulate excitatory synapse number through trans interactions with fibronectin leucine-rich repeat transmembrane 3 (FLRT3). By isothermal titration calorimetry, we determined that only the olfactomedin (OLF) domain of LPHN3 is necessary for FLRT3 association. By multi-crystal native single-wavelength anomalous diffraction phasing, we determined the crystal structure of the OLF domain. This structure is a five-bladed beta propeller with a Ca2+ ion bound in the central pore, which is capped by a mobile loop that allows the ion to exchange with the solvent. The crystal structure of the OLF/FLRT3 complex shows that LPHN3-OLF in the closed state binds with high affinity to the concave face of FLRT3-LRR with a combination of hydrophobic and charged residues. Our study provides structural and functional insights into the molecular mechanism underlying the contribution of LPHN3/FLRT3 to the development of glutamatergic synapses.

Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development.,Ranaivoson FM, Liu Q, Martini F, Bergami F, von Daake S, Li S, Lee D, Demeler B, Hendrickson WA, Comoletti D Structure. 2015 Jul 28. pii: S0969-2126(15)00275-0. doi:, 10.1016/j.str.2015.06.022. PMID:26235031^[5]

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

References

↑ O'Sullivan ML, de Wit J, Savas JN, Comoletti D, Otto-Hitt S, Yates JR 3rd, Ghosh A. FLRT proteins are endogenous latrophilin ligands and regulate excitatory synapse development. Neuron. 2012 Mar 8;73(5):903-10. doi: 10.1016/j.neuron.2012.01.018. PMID:22405201 doi:http://dx.doi.org/10.1016/j.neuron.2012.01.018
↑ O'Sullivan ML, Martini F, von Daake S, Comoletti D, Ghosh A. LPHN3, a presynaptic adhesion-GPCR implicated in ADHD, regulates the strength of neocortical layer 2/3 synaptic input to layer 5. Neural Dev. 2014 Apr 17;9:7. doi: 10.1186/1749-8104-9-7. PMID:24739570 doi:http://dx.doi.org/10.1186/1749-8104-9-7
↑ Jackson VA, Del Toro D, Carrasquero M, Roversi P, Harlos K, Klein R, Seiradake E. Structural Basis of Latrophilin-FLRT Interaction. Structure. 2015 Feb 17. pii: S0969-2126(15)00037-4. doi:, 10.1016/j.str.2015.01.013. PMID:25728924 doi:http://dx.doi.org/10.1016/j.str.2015.01.013
↑ Ranaivoson FM, Liu Q, Martini F, Bergami F, von Daake S, Li S, Lee D, Demeler B, Hendrickson WA, Comoletti D. Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development. Structure. 2015 Jul 28. pii: S0969-2126(15)00275-0. doi:, 10.1016/j.str.2015.06.022. PMID:26235031 doi:http://dx.doi.org/10.1016/j.str.2015.06.022
↑ Ranaivoson FM, Liu Q, Martini F, Bergami F, von Daake S, Li S, Lee D, Demeler B, Hendrickson WA, Comoletti D. Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development. Structure. 2015 Jul 28. pii: S0969-2126(15)00275-0. doi:, 10.1016/j.str.2015.06.022. PMID:26235031 doi:http://dx.doi.org/10.1016/j.str.2015.06.022

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/4rml"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4rml is ON HOLD  until Paper Publication
+==Crystal structure of the Olfactomedin domain of latrophilin 3 in C2221 crystal form==
+<StructureSection load='4rml' size='340' side='right'caption='[[4rml]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4rml]] is a 1 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=4RML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RML 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]] 1.601&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4rml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rml OCA], [https://pdbe.org/4rml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rml RCSB], [https://www.ebi.ac.uk/pdbsum/4rml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rml ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AGRL3_MOUSE AGRL3_MOUSE] Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25728924, PubMed:26235031). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570).<ref>PMID:22405201</ref> <ref>PMID:24739570</ref> <ref>PMID:25728924</ref> <ref>PMID:26235031</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Latrophilins (LPHNs) are adhesion-like G-protein-coupled receptors implicated in attention-deficit/hyperactivity disorder. Recently, LPHN3 was found to regulate excitatory synapse number through trans interactions with fibronectin leucine-rich repeat transmembrane 3 (FLRT3). By isothermal titration calorimetry, we determined that only the olfactomedin (OLF) domain of LPHN3 is necessary for FLRT3 association. By multi-crystal native single-wavelength anomalous diffraction phasing, we determined the crystal structure of the OLF domain. This structure is a five-bladed beta propeller with a Ca2+ ion bound in the central pore, which is capped by a mobile loop that allows the ion to exchange with the solvent. The crystal structure of the OLF/FLRT3 complex shows that LPHN3-OLF in the closed state binds with high affinity to the concave face of FLRT3-LRR with a combination of hydrophobic and charged residues. Our study provides structural and functional insights into the molecular mechanism underlying the contribution of LPHN3/FLRT3 to the development of glutamatergic synapses.
-Authors: Ranaivoson, F.M., Liu, Q., Martini, F., Bergami, F., Von daake, S., Li, S., Demeler, B., Hendrickson, W.A., Comoletti, D.
+Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development.,Ranaivoson FM, Liu Q, Martini F, Bergami F, von Daake S, Li S, Lee D, Demeler B, Hendrickson WA, Comoletti D Structure. 2015 Jul 28. pii: S0969-2126(15)00275-0. doi:, 10.1016/j.str.2015.06.022. PMID:26235031<ref>PMID:26235031</ref>
-Description: Crystal structure of the Olfactomedin domain of latrophilin 3 in C2221 crystal form
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4rml" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Latrophilin|Latrophilin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Bergami F]]
+[[Category: Comoletti D]]
+[[Category: Demeler B]]
+[[Category: Hendrickson WA]]
+[[Category: Li S]]
+[[Category: Liu Q]]
+[[Category: Martini F]]
+[[Category: Ranaivoson FM]]
+[[Category: Von daake S]]

4rml

From Proteopedia

Current revision

Crystal structure of the Olfactomedin domain of latrophilin 3 in C2221 crystal form

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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