Premium
Crystallographic refinement of human serum retinol binding protein at 2Å resolution
Author(s) -
Cowan Sandra W.,
Newcomer Marcia E.,
Jones T. Alwyn
Publication year - 1990
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340080108
Subject(s) - retinol binding protein , resolution (logic) , ligand (biochemistry) , chemistry , retinol , sequence (biology) , crystallography , biochemistry , computer science , vitamin , receptor , artificial intelligence
Human serum retinol binding protein (RBP) in complex with retinol has been crystallographically refined to an R‐factor of 18.1% with 2Å resolution data. The protein topology results in an anti‐parallel β‐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.