5afb

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the Latrophilin3 Lectin and Olfactomedin Domains

Structural highlights

5afb is a 1 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 2.16Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AGRL3_HUMAN 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:26235030). Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex.[UniProtKB:Q80TS3]^[1]

Publication Abstract from PubMed

Latrophilins, receptors for spider venom alpha-latrotoxin, are adhesion type G-protein-coupled receptors with emerging functions in synapse development. The N-terminal region binds the endogenous cell adhesion molecule FLRT, a major regulator of cortical and synapse development. We present crystallographic data for the mouse Latrophilin3 lectin and olfactomedin-like (Olf) domains, thereby revealing the Olf beta-propeller fold and conserved calcium-binding site. We locate the FLRT-Latrophilin binding surfaces by a combination of sequence conservation analysis, point mutagenesis, and surface plasmon resonance experiments. In stripe assays, we show that wild-type Latrophilin3 and its high-affinity interactor FLRT2, but not the binding-impaired mutants we generated, promote HeLa cell adhesion. In contrast, cortical neurons expressing endogenous FLRTs are repelled by wild-type Latrophilin3 and not by the binding-impaired mutant. Taken together, we present molecular level insights into Latrophilin structure, its FLRT-binding mechanism, and a role for Latrophilin and FLRT that goes beyond a simply adhesive interaction.

Structural Basis of Latrophilin-FLRT Interaction.,Jackson VA, Del Toro D, Carrasquero M, Roversi P, Harlos K, Klein R, Seiradake E Structure. 2015 Feb 17. pii: S0969-2126(15)00037-4. doi:, 10.1016/j.str.2015.01.013. PMID:25728924^[2]

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

References

↑ Lu YC, Nazarko OV, Sando R 3rd, Salzman GS, Sudhof TC, Arac D. Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion. Structure. 2015 Jul 28. pii: S0969-2126(15)00277-4. doi:, 10.1016/j.str.2015.06.024. PMID:26235030 doi:http://dx.doi.org/10.1016/j.str.2015.06.024
↑ 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

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/5afb"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Latrophilin3 Lectin and Olfactomedin Domains==
-<StructureSection load='5afb' size='340' side='right' caption='[[5afb]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
+<StructureSection load='5afb' size='340' side='right'caption='[[5afb]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5afb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AFB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5afb]] is a 1 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=5AFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AFB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.16&#8491;</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=5afb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afb OCA], [http://pdbe.org/5afb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5afb RCSB], [http://www.ebi.ac.uk/pdbsum/5afb PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5afb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afb OCA], [https://pdbe.org/5afb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5afb RCSB], [https://www.ebi.ac.uk/pdbsum/5afb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5afb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[https://www.uniprot.org/uniprot/AGRL3_HUMAN AGRL3_HUMAN] 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:26235030). Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex.[UniProtKB:Q80TS3]<ref>PMID:26235030</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5afb" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Latrophilin|Latrophilin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Carrasquero, M]]
+[[Category: Homo sapiens]]
-[[Category: Harlos, K]]
+[[Category: Large Structures]]
-[[Category: Jackson, V A]]
+[[Category: Carrasquero M]]
-[[Category: Klein, R]]
+[[Category: Harlos K]]
-[[Category: Roversi, P]]
+[[Category: Jackson VA]]
-[[Category: Seiradake, E]]
+[[Category: Klein R]]
-[[Category: Toro, D del]]
+[[Category: Roversi P]]
-[[Category: Adhesion]]
+[[Category: Seiradake E]]
-[[Category: Beta propeller]]
+[[Category: Del Toro D]]
-[[Category: Guidance]]
-[[Category: Lectin]]
-[[Category: Olfactomedin]]
-[[Category: Repulsion]]
-[[Category: Signaling protein]]

5afb

From Proteopedia

Current revision

Crystal structure of the Latrophilin3 Lectin and Olfactomedin Domains

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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