8FYU: Human CHIP-TPR domain

Name: PDB 8FYU: Crystal structure of the human CHIP-TPR domain in complex with a 10mer acetylated tau peptide
Published: 2023-08-30
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Crystal structure of the human CHIP-TPR domain in complex with a 10mer acetylated tau peptide. Determined by X-ray diffraction at 1.85 Å resolution. Released 30 Aug 2023.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,356
Mol. weight: 31.35 kDa
Released: 30 Aug 2023

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

Secondary structure: helices and β-sheets

8FYU contains 15 α-helices and 2 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.

Chain A: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	27-39	13
α-helix	43-56	14
α-helix	61-73	13
α-helix	77-90	14
α-helix	95-107	13
α-helix	111-127	17
β-strand	131	1	1
α-helix	135-149	15

Chain B: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	27-39	13
α-helix	43-56	14
α-helix	61-73	13
α-helix	77-90	14
α-helix	95-107	13
α-helix	111-127	17
α-helix	135-149	15

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	635	1	1

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	636-637	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase CHIP	A, B	protein	128	Homo sapiens	Q9UNE7 (AlphaFold model)
Ace-ser-ser-thr-gly-ser-ile-asp-met-val-asp	C, E	protein	10	Homo sapiens	P10636 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8FYU_1 E3 ubiquitin-protein ligase CHIP (chains A, B)
KSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALA
DCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRI
AKKKRWNS

Sequence of entity 2 (C, E), FASTA

>8FYU_2 ACE-SER-SER-THR-GLY-SER-ILE-ASP-MET-VAL-ASP (chains C, E)
SSTGSIDMVD

Primary citation

Phosphorylation of tau at a single residue inhibits binding to the E3 ubiquitin ligase, CHIP. Nadel, C.M., Pokhrel, S., Wucherer, K. et al. Nat Commun (2024) 15:7972-7972. DOI 10.1038/s41467-024-52075-1 · PubMed

Other PDB entries of the same protein (UniProt Q9UNE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9QFY 1.06 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 9.
6NSV 1.3 Å, Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated…
9QFS 1.33 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 8.
9QEU 1.35 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 1
8GCK 1.37 Å, Crystal structure of the human CHIP-TPR domain in complex with a 6mer acetylated tau…
8EI0 1.47 Å, Crystal structure of the STUB1 TPR domain in complex with H318, a Helicon Polypeptide
6EFK 1.5 Å, Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated HSP70…
9QF1 1.51 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 2
8F16 1.56 Å, Structure of the STUB1 TPR domain in complex with H203, an all-D Helicon Polypeptide
9DYB 1.6 Å, CHIP-TPR in complex with the phosphorylated Hsp70 tail
8SUV 1.63 Å, CHIP-TPR in complex with the C-terminus of CHIC2
8F14 1.69 Å, Structure of the STUB1 TPR domain in complex with H201, an all-D Helicon Polypeptide

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