› 4cq1

X-ray diffraction
1.69Å resolution

Crystal structure of the neuronal isoform of PTB

Released:
DOI: 10.2210/pdb4cq1/pdb
PDB entry 4cq1 coloured by chain, front view.
PDB entry 4cq1 coloured by chain, side view.
PDB entry 4cq1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB).
Joshi A, Esteve V, Buckroyd AN, Blatter M, Allain FH, Curry S
OpenAccess logo PeerJ 2 e305 (2014)
PMID: 24688880

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-577511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polypyrimidine tract-binding protein 2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 196 amino acids
Theoretical weight: 21.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UKA9 (Residues: 336-531; Coverage: 37%)
Gene names: NPTB, PTB, PTBLP, PTBP2
Sequence domains:
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:
Ligand ZN 12 x ZN
Ligand CL 8 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 61Å b: 65.81Å c: 99.58Å
α: 89.99° β: 90° γ: 89.99°
R-values:
R R work R free
0.172 0.17 0.208
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Multiple determinants of splicing repression activity in the polypyrimidine tract binding proteins, PTBP1 and PTBP2.
Keppetipola et al. (2016)
5 more

3 mentions without citation

Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.
Lapkouski et al. (2015)
2 more