8C17: TEAD4

Crystal structure of TEAD4 in complex with peptide 1. Determined by X-ray diffraction at 2.25 Å resolution. Released 15 Mar 2023.

Method: X-ray diffraction
Resolution: 2.25 Å
Organisms: Homo sapiens, Synthetic construct
Chains: 2
Atoms: 1,976
Mol. weight: 28.26 kDa
Ligands: MYR
Released: 15 Mar 2023

Explore 8C17 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8C17 contains 8 α-helices and 17 β-strands across 2 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, 17 β-strands

Element	Residues	Length	Sheet
β-strand	216	1	1
β-strand	219-220	2	2
β-strand	225-238	14	2
β-strand	241-250	10	2
β-strand	257	1	1
β-strand	259	1	3
β-strand	262	1	3
β-strand	264-266	3	4
α-helix	267-269	3
α-helix	271-273	3
α-helix	281-287	7
α-helix	290-292	3
β-strand	293-300	8	4
β-strand	311-322	12	2
β-strand	328-336	9	4
β-strand	339-348	10	4
β-strand	351-353	3	2
β-strand	356-365	10	2
α-helix	366-367	2
α-helix	368-378	11
α-helix	383-390	8
β-strand	393-401	9	4
β-strand	407-417	11	4
β-strand	425-432	8	4

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-12	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A	protein	220	Homo sapiens	Q15561 (AlphaFold model)
Stapled peptide	B	protein	19	Synthetic construct

Sequence of entity 1 (A), FASTA

>8C17_1 Transcriptional enhancer factor TEF-3 (chains A)
GPRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYDKF
PEKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCSTKV
CSFGKQVVEKVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFT
ILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (B), FASTA

>8C17_2 Stapled peptide (chains B)
XFSPADFHXDIACDVARGX

Ligands and cofactors

ID	Name	Formula	Copies
MYR	Myristic acid	C14 H28 O2	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Biochemical and Structural Characterization of a Peptidic Inhibitor of the YAP:TEAD Interaction That Binds to the alpha-Helix Pocket on TEAD. Mesrouze, Y., Gubler, H., Villard, F. et al. ACS Chem Biol (2023) 18:643-651. DOI 10.1021/acschembio.2c00936 · PubMed

Other PDB entries of the same protein (UniProt Q15561 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SYN 1.3 Å, Crystal structure of TEAD4 in complex with Vgll1-peptide and IAG933
6GEI 1.65 Å, TEAD4 (216-434);E263A+Y429F complexed with yap peptide (60- 100);S94A and myristoate…
6HIK 1.65 Å, X-ray structure of TEAD4(Y429H) mutant) complexed with YAP (wildtype): Molecular and…
6SEN 1.65 Å, TEAD4 bound to a FAM181A peptide
8A8R 1.7 Å, Crystal structure of TEAD4 in complex with YAP peptide
6GEC 1.7 Å, TEAD4 (216-434) complexed with yap peptide (60-100);S94A and myristoate (covalently…
9QKQ 1.74 Å, Crystal structure of hTEAD4 YAP binding domain (hTEAD4-YBD) in complex with peptide 6
6GE6 1.8 Å, X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of…
6GE3 1.85 Å, X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual…
5OAQ 1.95 Å, TEAD4 complexed with yap peptide and myristate (covalently bound)
6GEE 1.96 Å, TEAD4 (216-434);E263A complexed with yap peptide (60-100); S94A and myristoate…
6GE4 1.97 Å, TEAD4 (216-434);E263A complexed with yap peptide (60-100) and myristoate (covalently…

Browse structure collections

About this viewer

MolViewer shows 8C17 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.