› 1ytv

X-ray diffraction
1.8Å resolution

Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor

Released:
DOI: 10.2210/pdb1ytv/pdb
PDB 1ytv coloured by chain and viewed from the front.
PDB 1ytv coloured by chain and viewed from the side.
PDB 1ytv coloured by chain and viewed from the top.
Source organisms:
Primary publication:
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.
Adikesavan NV, Mahmood SS, Stanley N, Xu Z, Wu N, Thibonnier M, Shoham M
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 341-5 (2005)
PMID: 16511036

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Maltose/maltodextrin-binding periplasmic protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 40.25 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II
Vasopressin V1a receptor Chains: M, N
Molecule details ›
Chains: M, N
Length: 84 amino acids
Theoretical weight: 9.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P37288 (Residues: 361-361, 362-418; Coverage: 14%)
Gene names: AVPR1, AVPR1A
Sequence domains: Domain of unknown function (DUF1856)

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 51.102Å b: 66.557Å c: 115.723Å
α: 90° β: 95.99° γ: 90°
R-values:
R R work R free
0.196 0.199 0.225
Expression system: Escherichia coli BL21

Quick links

Citations

4 citation in other articles

Site-specific protein modification through Cu(I)-catalyzed 1,2,3-triazole formation and its implementation in protein microarray fabrication.
Lin et al. (2006)
3 more

2 mentions without citation

Intrinsically semi-disordered state and its role in induced folding and protein aggregation.
Zhang et al. (2013)
1 more