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5cmp

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human FLRT3 LRR domain

Structural highlights

5cmp is a 4 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 2.601Å
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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

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

@@ Line 1: / Line 1: @@
 ==human FLRT3 LRR domain==
-<StructureSection load='5cmp' size='340' side='right' caption='[[5cmp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='5cmp' size='340' side='right'caption='[[5cmp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5cmp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CMP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CMP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5cmp]] is a 4 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=5CMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CMP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.601&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cmn|5cmn]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmp OCA], [http://pdbe.org/5cmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cmp RCSB], [http://www.ebi.ac.uk/pdbsum/5cmp PDBsum]</span></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=5cmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmp OCA], [https://pdbe.org/5cmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cmp RCSB], [https://www.ebi.ac.uk/pdbsum/5cmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmp ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://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>
+[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 ==
-[[http://www.uniprot.org/uniprot/FLRT3_HUMAN FLRT3_HUMAN]] May have a function in cell adhesion and/or receptor signaling.
+[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 ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Arac, D]]
+[[Category: Homo sapiens]]
-[[Category: Lu, Y]]
+[[Category: Large Structures]]
-[[Category: Salzman, G]]
+[[Category: Arac D]]
-[[Category: Cell adhesion]]
+[[Category: Lu Y]]
-[[Category: Lrr repeat]]
+[[Category: Salzman G]]

5cmp

From Proteopedia

Current revision

human FLRT3 LRR domain

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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