PDBe 1xr0

Solution NMR

Structural Basis of SNT PTB Domain Interactions with Distinct Neurotrophic Receptors

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fibroblast growth factor receptor 1 Chain: A
Molecule details ›
Chain: A
Length: 22 amino acids
Theoretical weight: 2.49 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P11362 (Residues: 409-430; Coverage: 3%)
Gene names: BFGFR, CEK, FGFBR, FGFR1, FLG, FLT2, HBGFR
Fibroblast growth factor receptor substrate 2 Chain: B
Molecule details ›
Chain: B
Length: 129 amino acids
Theoretical weight: 15.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WU20 (Residues: 11-136; Coverage: 25%)
Gene name: FRS2
Sequence domains: PTB domain (IRS-1 type)
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Structures of the SNT-1 PTB domain in complex with the hFGFR1 peptide were calculated with a distance geometry and simulated annealing protocol by using the X-PLOR program ([4]). NOE distance and dihedral angle restraints were treated with a square-well potential of 50 kcal mol?1 ?2. A total of 2448 manually assigned NOE-derived distance restraints were obtained from the 15N- or 13C-edited NOESY data. Included in this figure are 251 intrapeptide and 258 intermolecular distance restraints. Additionally, 255 unambiguous and 52 ambiguous distance restraints were identified from the NOE data by using ARIA. The final structure calculations employed a total of 2755 NOE restraints obtained from the manual and the ARIA-assisted assignments, 2703 of which were unambiguously assigned NOE-derived distance restraints that comprise 1072 intraresidue, 466 sequential, 216 medium-range, and 949 long-range NOEs. In addition, 70 hydrogen-bond distance restraints for 35 hydrogen bonds and 19 -angle restraints were also used in the structure calculations. For the ensemble of the final 20 structures, no distance or torsional angle restraint was violated by more than 0.4 or 5, respectively. The distance-violation, dihedral-violation, and total energies were 74.4 1.7 kcal mol/1, 0.82 0.08 kcal mol/1, and 262.0 6.0 kcal mol/1, respectively. The Lennard-Jones potential, which was not used during any refinement stage, was 659.3 23.1 kcal mol/1 for the final structures. Ramachandran plot analysis by Procheck-NMR showed that in the final structures of the complex, 98.1% of the backbone geometries of the non-Gly and non-Pro residues in the complex (protein residues 18-116 and peptide residues (412-430) and nearly 100% in the secondary structure (protein residues 19-24, 35-40, 45-49, 52-57, 63-68, 71-76, 85-90, 94-107, and 111-115 and peptide residues 426-430) lie within energetically favorable or allowed regions.
Expression systems:
  • Not provided
  • Escherichia coli