5cmn

From Proteopedia

(Difference between revisions)

Current revision

FLRT3 LRR domain in complex with LPHN3 Olfactomedin domain

Structural highlights

5cmn is a 8 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 3.605Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

FLRT3_HUMAN Kallmann syndrome. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FLRT3 also have a mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17 (PubMed:23643382).^[1]

Function

FLRT3_HUMAN May have a function in cell adhesion and/or receptor signaling.

Publication Abstract from PubMed

Fibronectin leucine-rich repeat transmembrane proteins (FLRTs) are cell-adhesion molecules with emerging functions in cortical development and synapse formation. Their extracellular regions interact with latrophilins (LPHNs) to mediate synapse development, and with Uncoordinated-5 (UNC5)/netrin receptors to control the migration of neurons in the developing cortex. Here, we present the crystal structures of FLRT3 in isolation and in complex with LPHN3. The LPHN3/FLRT3 structure reveals that LPHN3 binds to FLRT3 at a site distinct from UNC5. Structure-based mutations specifically disrupt LPHN3/FLRT3 binding, but do not disturb their interactions with other proteins or their cell-membrane localization. Thus, they can be used as molecular tools to dissect the functions of FLRTs and LPHNs in vivo. Our results suggest that UNC5 and LPHN3 can simultaneously bind to FLRT3, forming a trimeric complex, and that FLRT3 may form transsynaptic complexes with both LPHN3 and UNC5. These findings provide molecular insights for understanding the role of cell-adhesion proteins in synapse function.

Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion.,Lu YC, Nazarko OV, Sando R 3rd, Salzman GS, Sudhof TC, Arac D Structure. 2015 Jul 28. pii: S0969-2126(15)00277-4. doi:, 10.1016/j.str.2015.06.024. PMID:26235030^[2]

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

References

↑ Miraoui H, Dwyer AA, Sykiotis GP, Plummer L, Chung W, Feng B, Beenken A, Clarke J, Pers TH, Dworzynski P, Keefe K, Niedziela M, Raivio T, Crowley WF Jr, Seminara SB, Quinton R, Hughes VA, Kumanov P, Young J, Yialamas MA, Hall JE, Van Vliet G, Chanoine JP, Rubenstein J, Mohammadi M, Tsai PS, Sidis Y, Lage K, Pitteloud N. Mutations in FGF17, IL17RD, DUSP6, SPRY4, and FLRT3 are identified in individuals with congenital hypogonadotropic hypogonadism. Am J Hum Genet. 2013 May 2;92(5):725-43. doi: 10.1016/j.ajhg.2013.04.008. PMID:23643382 doi:http://dx.doi.org/10.1016/j.ajhg.2013.04.008
↑ 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

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5cmn"

Categories: Homo sapiens | Large Structures | Arac D | Lu Y | Salzman G

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5cmn is ON HOLD
+==FLRT3 LRR domain in complex with LPHN3 Olfactomedin domain==
+<StructureSection load='5cmn' size='340' side='right'caption='[[5cmn]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5cmn]] is a 8 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=5CMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CMN 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]] 3.605&#8491;</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=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=5cmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmn OCA], [https://pdbe.org/5cmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cmn RCSB], [https://www.ebi.ac.uk/pdbsum/5cmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmn ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/FLRT3_HUMAN FLRT3_HUMAN] Kallmann syndrome. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FLRT3 also have a mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17 (PubMed:23643382).<ref>PMID:23643382</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/FLRT3_HUMAN FLRT3_HUMAN] May have a function in cell adhesion and/or receptor signaling.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Fibronectin leucine-rich repeat transmembrane proteins (FLRTs) are cell-adhesion molecules with emerging functions in cortical development and synapse formation. Their extracellular regions interact with latrophilins (LPHNs) to mediate synapse development, and with Uncoordinated-5 (UNC5)/netrin receptors to control the migration of neurons in the developing cortex. Here, we present the crystal structures of FLRT3 in isolation and in complex with LPHN3. The LPHN3/FLRT3 structure reveals that LPHN3 binds to FLRT3 at a site distinct from UNC5. Structure-based mutations specifically disrupt LPHN3/FLRT3 binding, but do not disturb their interactions with other proteins or their cell-membrane localization. Thus, they can be used as molecular tools to dissect the functions of FLRTs and LPHNs in vivo. Our results suggest that UNC5 and LPHN3 can simultaneously bind to FLRT3, forming a trimeric complex, and that FLRT3 may form transsynaptic complexes with both LPHN3 and UNC5. These findings provide molecular insights for understanding the role of cell-adhesion proteins in synapse function.
-Authors: Lu, Y., Salzman, G., Arac, D.
+Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion.,Lu YC, Nazarko OV, Sando R 3rd, Salzman GS, Sudhof TC, Arac D Structure. 2015 Jul 28. pii: S0969-2126(15)00277-4. doi:, 10.1016/j.str.2015.06.024. PMID:26235030<ref>PMID:26235030</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Arac, D]]
+<div class="pdbe-citations 5cmn" style="background-color:#fffaf0;"></div>
-[[Category: Lu, Y]]
-[[Category: Salzman, G]]
+==See Also==
+*[[Latrophilin|Latrophilin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Arac D]]
+[[Category: Lu Y]]
+[[Category: Salzman G]]

5cmn

From Proteopedia

Current revision

FLRT3 LRR domain in complex with LPHN3 Olfactomedin domain

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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