› 5sxp

X-ray diffraction
1.65Å resolution

STRUCTURAL BASIS FOR THE INTERACTION BETWEEN ITCH PRR AND BETA-PIX

Released:
DOI: 10.2210/pdb5sxp/pdb
PDB entry 5sxp coloured by chain, front view.
PDB entry 5sxp coloured by chain, side view.
PDB entry 5sxp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis of interactions between SH3 domain-containing proteins and the proline-rich region of the ubiquitin ligase Itch.
Desrochers G, Cappadocia L, Lussier-Price M, Ton AT, Ayoubi R, Serohijos A, Omichinski JG, Angers A
J Biol Chem 292 6325-6338 (2017)
PMID: 28235806

Function and Biology Details

Reaction catalysed: 
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171944 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Rho guanine nucleotide exchange factor 7 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 62 amino acids
Theoretical weight: 7.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14155 (Residues: 183-243; Coverage: 8%)
Gene names: ARHGEF7, COOL1, KIAA0142, Nbla10314, P85SPR, PAK3BP, PIXB
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains
E3 ubiquitin-protein ligase Itchy homolog Chains: F, G
Molecule details ›
Chains: F, G
Length: 27 amino acids
Theoretical weight: 2.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96J02 (Residues: 249-269; Coverage: 2%)
Gene name: ITCH

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 28.845Å b: 43.451Å c: 61.482Å
α: 90.37° β: 101.01° γ: 105.25°
R-values:
R R work R free
0.14 0.139 0.161
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Endo-lysosomal dysregulations and late-onset Alzheimer's disease: impact of genetic risk factors.
Van Acker et al. (2019)
3 more

3 mentions without citation

Exploration of Aberrant E3 Ligases Implicated in Alzheimer's Disease and Development of Chemical Tools to Modulate Their Function.
Potjewyd et al. (2021)
2 more