4LN0: VGLL4-TEAD4 complex

Crystal structure of the VGLL4-TEAD4 complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 26 Feb 2014.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Mus musculus
Chains: 3
Atoms: 3,705
Mol. weight: 58.68 kDa
Released: 26 Feb 2014

Explore 4LN0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LN0 contains 23 α-helices and 27 β-strands across 3 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.

Chain A: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	213	1	1
β-strand	218-227	10	1
β-strand	237-244	8	1
α-helix	253-255	3
β-strand	256-259	4	2
α-helix	260-262	3
α-helix	264-266	3
α-helix	274-280	7
α-helix	283-285	3
β-strand	286-293	8	2
β-strand	306-315	10	1
β-strand	321-329	9	2
β-strand	332-341	10	2
α-helix	342-343	2
β-strand	344-346	3	1
β-strand	349-358	10	1
α-helix	359-360	2
α-helix	361-371	11
α-helix	376-384	9
β-strand	386-394	9	2
β-strand	400-410	11	2
β-strand	418-425	8	2

Chain B: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	213	1	3
β-strand	218-226	9	3
β-strand	238-243	6	3
β-strand	256-259	4	2
α-helix	260-262	3
α-helix	264-266	3
α-helix	274-280	7
α-helix	283-285	3
β-strand	286-293	8	2
β-strand	307-315	9	3
β-strand	321-329	9	2
β-strand	332-341	10	2
α-helix	342	1
β-strand	343-346	4	3
β-strand	349-358	10	3
α-helix	359-360	2
α-helix	361-371	11
α-helix	376-383	8
β-strand	386-394	9	2
β-strand	400-410	11	2
β-strand	418-425	8	2

Chain C: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	204-214	11
α-helix	215-217	3
α-helix	223	1
α-helix	225	1
β-strand	227-230	4	2
α-helix	234-242	9
α-helix	244-250	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A, B	protein	222	Mus musculus	Q62296 (AlphaFold model)
Transcription cofactor vestigial-like protein 4	C	protein	58	Mus musculus	Q80V24 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4LN0_1 Transcriptional enhancer factor TEF-3 (chains A, B)
STMGRSIASSKLWMLEFSAFLERQQDPDTYNKHLFVHISQSSPSYSDPYLETVDIRQIYD
KFPEKKGGLKELFERGPSNAFFLVKFWADLNTNIDDEGSAFYGVSSQYESPENMIITCST
KVCSFGKQVVEKVETEYARYENGHYLYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLEN
FTILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (C), FASTA

>4LN0_2 Transcription cofactor vestigial-like protein 4 (chains C)
STMGDPVVEEHFRRSLGKNYKEPEPAPNSVSITGSVDDHFAKALGDTWLQIKAAKDSA

Primary citation

A Peptide Mimicking VGLL4 Function Acts as a YAP Antagonist Therapy against Gastric Cancer. Jiao, S., Wang, H., Shi, Z. et al. Cancer Cell (2014) 25:166-180. DOI 10.1016/j.ccr.2014.01.010 · PubMed

Other PDB entries of the same protein (UniProt Q62296 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6SBA 1.3 Å, Crystal Structure of mTEAD with a VGL4 Tertiary Structure Mimetic
5XJD 2.22 Å, TEAD in complex with fragment
6L9F 2.56 Å, Crystal structure of TEAD4 in complex with a novel FAM181A peptide
5Z2Q 2.74 Å, Vgll1-TEAD4 core complex
5GN0 2.9 Å, Structure of TAZ-TEAD complex
3JUA 3.0 Å, Structural basis of YAP recognition by TEAD4 in the Hippo pathway

Browse structure collections

About this viewer

MolViewer shows 4LN0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.