4V2C: Mouse FLRT2 LRR domain

mouse FLRT2 LRR domain in complex with rat Unc5D Ig1 domain. Determined by X-ray diffraction at 4.0 Å resolution. Released 5 Nov 2014.

Method: X-ray diffraction
Resolution: 4.0 Å
Organisms: MUS MUSCULUS, RATTUS NORVEGICUS
Chains: 4
Atoms: 6,854
Mol. weight: 110.33 kDa
Released: 5 Nov 2014

Explore 4V2C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4V2C contains 29 α-helices and 74 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and C: 9 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	41-43	3	1
β-strand	46-48	3	1
β-strand	67-69	3	1
α-helix	82-84	3
β-strand	92-94	3	1
β-strand	102	1	2
α-helix	103-104	2
β-strand	113-115	3	1
β-strand	123	1	2
β-strand	124	1	3
α-helix	126-131	6
β-strand	137-139	3	1
β-strand	150	1	3
α-helix	155-157	3
β-strand	163-165	3	1
β-strand	173	1	4
β-strand	184-186	3	1
β-strand	194	1	4
β-strand	195	1	5
β-strand	208-210	3	1
β-strand	221	1	5
α-helix	222	1
β-strand	234-236	3	1
α-helix	245-246	2
β-strand	256-258	3	1
β-strand	280-282	3	1
β-strand	304-306	3	1
β-strand	312-313	2	6
α-helix	316-318	3
α-helix	319-327	9
β-strand	333-335	3	1
β-strand	338	1	7
β-strand	339-341	3	6
β-strand	349	1	7
α-helix	350-352	3

Chain B: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	53-56	4	8
α-helix	57-60	4
β-strand	61-63	3	9
α-helix	67-68	2
β-strand	69-76	8	8
β-strand	80-85	6	10
β-strand	88-89	2	10
α-helix	90-91	2
α-helix	92-94	3
β-strand	95-101	7	8
α-helix	107	1
β-strand	108-116	9	8
α-helix	118-123	6
β-strand	131-137	7	10
β-strand	142-144	3	10
β-strand	148-149	2	10
β-strand	150-152	3	9

Chain D: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	53-56	4	18
α-helix	57-60	4
β-strand	61-63	3	19
α-helix	67-68	2
β-strand	69-76	8	18
β-strand	80-85	6	20
β-strand	88-89	2	20
α-helix	92-94	3
β-strand	95-101	7	18
α-helix	107	1
β-strand	108-116	9	18
α-helix	118-123	6
β-strand	131-137	7	20
β-strand	142-144	3	20
β-strand	148-149	2	20
β-strand	150-152	3	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibronectin leucine rich transmembrane protein 2	A, C	protein	328	MUS MUSCULUS	Q8BLU0 (AlphaFold model)
Protein UNC5D	B, D	protein	161	RATTUS NORVEGICUS	F1LW30 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4V2C_1 FIBRONECTIN LEUCINE RICH TRANSMEMBRANE PROTEIN 2 (chains A, C)
ACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVY
LYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGA
FREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGN
LLTNKGIAEGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFAN
LRKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCDCSIKWVTEWLKYIPSSLNV
RGFMCQGPEQVRGMAVRELNMNLLSCPT

Sequence of entity 2 (B, D), FASTA

>4V2C_2 PROTEIN UNC5D (chains B, D)
MGTGAADRSRGARWWLPWLGLCFWAAGAEAARGADSGEVLPDSIPSAPGTLPHFIEEPED
AYIIKSNPIALRCKARPAMQIFFKCNGEWVHQNEHVSEESLDESSGLKVREVFINVTRQQ
VEDFHGPEDYWCQCVAWSHLGTSKSRKASVRIAYLRKNFEQ

Primary citation

Flrt Structure: Balancing Repulsion and Cell Adhesion in Cortical and Vascular Development. Seiradake, E., Del Toro, D., Nagel, D. et al. Neuron (2014) 84:370. DOI 10.1016/J.NEURON.2014.10.008 · PubMed

Other PDB entries of the same protein (UniProt Q8BLU0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4V2D 2.5 Å, FLRT2 LRR domain
5FTT 3.4 Å, Octameric complex of Latrophilin 3 (Lec, Olf) , Unc5D (Ig, Ig2, TSP1) and FLRT2 (LRR)
5FTU 6.01 Å, Tetrameric complex of Latrophilin 3, Unc5D and FLRT2

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