Crystallographic refinement of human serum retinol binding protein at 2A resolution.
Human serum retinol binding protein (RBP) in complex with retinol has been crystallographically refined to an R-factor of 18.1% with 2A resolution data. The protein topology results in an anti-parallel beta-barrel that encapsulates the retinol ligand. A detailed description of the protein and the binding site is provided. Our structural work has helped to define a family of proteins, many of which are carrier proteins for smaller ligand molecules. We describe the structural basis for the conservation of sequence within the family.
Cowan
S W
SW
Department of Molecular Biology, Biomedicum Centre, Uppsala, Sweden.
Newcomer
M E
ME
Jones
T A
TA
D000595:Amino Acid Sequence; D001665:Binding Sites; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011228:Prealbumin / Q000378:metabolism; D011487:Protein Conformation; D012177:Retinol-Binding Proteins / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid; D014801:Vitamin A / Q000378:metabolism; D014961:X-Ray Diffraction
D011228:Prealbumin; D012177:Retinol-Binding Proteins; D014801:Vitamin A