Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor.

Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M, J Mol Biol 373(5):1269-80 (2007) Europe PMC

SASDH43 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1
MWI(0) 67 kDa
MWexpected 70 kDa
VPorod 135 nm3
log I(s) 1.40×102 1.40×101 1.40×100 1.40×10-1
N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 small angle scattering data  s, nm-1
ln I(s)
N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 Guinier plot ln 1.40×102 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 Kratky plot 1.104 0 3 sRg
p(r)
N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 pair distance distribution function Rg: 3.3 nm 0 Dmax: 10 nm

Data validation


Fits and models


log I(s)
 s, nm-1
N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 BUNCH model

X-ray scattering data from the from the N-terminal domains of the inositol 1,4,5-triphosphate receptor type I (IP3R) in 15 mM Tris-HCl 300 mM NaCl 1 mM TCEP 5 mM EGTA pH 8.0 were collected on a Bruker Nanostar instrument at the Bragg Institute (Australian Nuclear Science and Technology Organisation, Lucas Heights, Australia) using a HiStar 2D detector (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle; λ=0.15406 nm). Approximately 15 µL of a 2.5 mg/ml protein solution was loaded into a quartz capillary mounted in a stainless steel holder. A single 3600s second frame was collected, and the buffer was collected in an analogous fashion. The data were normalized to the intensity of the transmitted beam, radially averaged, and the scattering of the solvent-blank was subtracted. The data are on an arbitrary scale, and the mass of the protein was determined using a lysozyme secondary standard at a concentration of 5.5 mg/ml. The model and corresponding fits include are derived from a rigid body model using BUNCH05.

Model derived from PDB structures 1XZZ and 1N4K (which is missing many residues).

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3R1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   70.5 kDa
 
UniProt   P11881 (1-604)
Sequence   FASTA
 
PDB ID   1XZZ
 
PDB ID   1N4K