3JUA: YAP recognition by TEAD4 in the Hippo pathway

Structural basis of YAP recognition by TEAD4 in the Hippo pathway. Determined by X-ray diffraction at 3.0 Å resolution. Released 23 Feb 2010.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Mus musculus
Chains: 8
Atoms: 8,055
Mol. weight: 120.89 kDa
Released: 23 Feb 2010

Explore 3JUA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3JUA contains 38 α-helices and 52 β-strands across 8 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: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	213	1	1
β-strand	218-228	11	1
β-strand	233-242	10	1
α-helix	254-256	3
β-strand	257-259	3	2
α-helix	260-262	3
α-helix	264-266	3
α-helix	274-280	7
β-strand	286-293	8	2
β-strand	305-315	11	1
β-strand	320-329	10	2
β-strand	332-342	11	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	376-383	8
β-strand	386-394	9	2
β-strand	400-410	11	2
β-strand	418-425	8	2

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	51-58	8
α-helix	71-73	3
α-helix	79-81	3

Chain C: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	213	1	3
β-strand	218-229	12	3
β-strand	233-242	10	3
β-strand	256-259	4	4
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	4
α-helix	299-301	3
β-strand	306-315	10	3
β-strand	320-329	10	4
β-strand	332-342	11	4
β-strand	344-345	2	3
β-strand	350-354	5	3
α-helix	361-370	10
α-helix	376-384	9
β-strand	386-394	9	4
β-strand	400-410	11	4
β-strand	418-425	8	4

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	51-54	4
α-helix	78-81	4

Chain E: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	213	1	5
β-strand	218-228	11	5
β-strand	234-240	7	5
α-helix	253-255	3
β-strand	256-259	4	6
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	6
β-strand	306-315	10	5
β-strand	321-328	8	6
β-strand	333-341	9	6
β-strand	344-346	3	5
β-strand	349-358	10	5
α-helix	359-360	2
α-helix	361-371	11
α-helix	376-383	8
β-strand	387-394	8	6
β-strand	400-410	11	6
β-strand	418-425	8	6

Chain F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	50-53	4
α-helix	55-57	3
α-helix	71-73	3
α-helix	78-80	3

Chain G: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	213	1	1
β-strand	218-229	12	1
β-strand	233-241	9	1
β-strand	257-259	3	7
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	7
β-strand	308-315	8	1
β-strand	320-326	7	7
β-strand	339-342	4	7
β-strand	345	1	1
β-strand	350-354	5	1
α-helix	361-371	11
α-helix	376-382	7
β-strand	387-394	8	7
β-strand	400-410	11	7
β-strand	418-425	8	7

Chain H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	78-80	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A, C, E, G	protein	220	Mus musculus	Q62296 (AlphaFold model)
65 kDa Yes-associated protein	B, D, F, H	protein	39	Mus musculus	P46938 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>3JUA_1 Transcriptional enhancer factor TEF-3 (chains A, C, E, G)
SMRSIASSKLWMLEFSAFLERQQDPDTYNKHLFVHISQSSPSYSDPYLETVDIRQIYDKF
PEKKGGLKELFERGPSNAFFLVKFWADLNTNIDDEGSAFYGVSSQYESPENMIITCSTKV
CSFGKQVVEKVETEYARYENGHYLYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFT
ILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (B, D, F, H), FASTA

>3JUA_2 65 kDa Yes-associated protein (chains B, D, F, H)
ETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPE

Primary citation

Structural basis of YAP recognition by TEAD4 in the hippo pathway. Chen, L., Chan, S.W., Zhang, X. et al. Genes Dev (2010) 24:290-300. DOI 10.1101/gad.1865310 · 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
4LN0 2.9 Å, Crystal structure of the VGLL4-TEAD4 complex
5GN0 2.9 Å, Structure of TAZ-TEAD complex

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