5GN0: TAZ-TEAD complex

Structure of TAZ-TEAD complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 May 2017.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Mus musculus
Chains: 8
Atoms: 8,228
Mol. weight: 123.15 kDa
Ligands: PLM, CIT
Released: 31 May 2017

Explore 5GN0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5GN0 contains 49 α-helices and 56 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	234-243	10	1
α-helix	253-255	3
β-strand	256-258	3	2
α-helix	260-266	7
α-helix	274-280	7
α-helix	283-285	3
β-strand	286-293	8	2
β-strand	306-315	10	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	418-424	7	2

Chain B: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	207-210	4
β-strand	213	1	1
β-strand	218-229	12	1
β-strand	234-244	11	1
α-helix	253-255	3
β-strand	256-258	3	3
α-helix	260-266	7
α-helix	274-280	7
α-helix	283-285	3
β-strand	286-292	7	3
β-strand	293	1	4
α-helix	299-301	3
β-strand	306-315	10	1
β-strand	321-329	9	3
β-strand	332-341	10	3
β-strand	344-346	3	1
β-strand	349-358	10	1
α-helix	359-360	2
α-helix	361-371	11
α-helix	376-382	7
α-helix	383-385	3
β-strand	386-394	9	3
β-strand	400-407	8	3
β-strand	410	1	4
β-strand	418-424	7	3

Chain C: 11 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	207-209	3
β-strand	213	1	5
β-strand	218-229	12	5
β-strand	234-244	11	5
α-helix	253-255	3
β-strand	256-258	3	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
α-helix	299-302	4
β-strand	306-315	10	5
β-strand	321-329	9	6
β-strand	332-341	10	6
β-strand	344-346	3	5
β-strand	349-358	10	5
α-helix	359-360	2
α-helix	361-370	10
α-helix	376-382	7
α-helix	383-385	3
β-strand	386-394	9	6
β-strand	400-410	11	6
β-strand	418-424	7	6

Chain D: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	207-209	3
β-strand	213	1	5
β-strand	218-228	11	5
β-strand	234-243	10	5
α-helix	253-255	3
β-strand	256-258	3	7
α-helix	260-266	7
α-helix	274-280	7
α-helix	283-285	3
β-strand	286-293	8	7
β-strand	306-315	10	5
β-strand	320-329	10	7
β-strand	332-342	11	7
β-strand	344-346	3	5
β-strand	349-358	10	5
α-helix	359-360	2
α-helix	361-370	10
α-helix	376-382	7
α-helix	383-385	3
β-strand	386-394	9	7
β-strand	400-410	11	7
β-strand	418-424	7	7

Chain E: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	29-31	3
β-strand	33	1	8
β-strand	36	1	8
α-helix	38-40	3
α-helix	43-45	3
α-helix	50-52	3

Chain F: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	40-42	3
α-helix	50-53	4

Chain G: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	29-32	4
α-helix	38-41	4
α-helix	50-52	3

Chain H: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	31-33	3
α-helix	43-45	3
α-helix	50-53	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A, B, C, D	protein	225	Mus musculus	Q62296 (AlphaFold model)
WW domain-containing transcription regulator protein 1	E, F, G, H	protein	35	Mus musculus	Q9EPK5 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5GN0_1 Transcriptional enhancer factor TEF-3 (chains A, B, C, D)
DLNWISMRSIASSKLWMLEFSAFLERQQDPDTYNKHLFVHISQSSPSYSDPYLETVDIRQ
IYDKFPEKKGGLKELFERGPSNAFFLVKFWADLNTNIDDEGSAFYGVSSQYESPENMIIT
CSTKVCSFGKQVVEKVETEYARYENGHYLYRIHRSPLCEYMINFIHKLKHLPEKYMMNSV
LENFTILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (E, F, G, H), FASTA

>5GN0_2 WW domain-containing transcription regulator protein 1 (chains E, F, G, H)
PLDTDLEALFNSVMNPKPSSWRKKILPESFFKEPD

Ligands and cofactors

ID	Name	Formula	Copies
PLM	Palmitic acid	C16 H32 O2	3
CIT	Citric acid	C6 H8 O7	2

Primary citation

Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex. Kaan, H.Y.K., Chan, S.W., Tan, S.K.J. et al. Sci Rep (2017) 7:2035-2035. DOI 10.1038/s41598-017-02219-9 · 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
3JUA 3.0 Å, Structural basis of YAP recognition by TEAD4 in the Hippo pathway

Browse structure collections

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