1RBP
CRYSTALLOGRAPHIC REFINEMENT OF HUMAN SERUM RETINOL BINDING PROTEIN AT 2 ANGSTROMS RESOLUTION
Summary for 1RBP
Entry DOI | 10.2210/pdb1rbp/pdb |
Descriptor | PLASMA RETINOL-BINDING PROTEIN PRECURSOR, RETINOL (3 entities in total) |
Functional Keywords | retinol transport |
Biological source | Homo sapiens (human) |
Cellular location | Secreted : P02753 |
Total number of polymer chains | 1 |
Total formula weight | 21270.90 |
Authors | Jones, T.A.,Newcomer, M.E.,Cowan, S.W. (deposition date: 1990-04-02, release date: 1991-07-15, Last modification date: 2024-11-06) |
Primary citation | Cowan, S.W.,Newcomer, M.E.,Jones, T.A. Crystallographic refinement of human serum retinol binding protein at 2A resolution. Proteins, 8:44-61, 1990 Cited by PubMed Abstract: 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. PubMed: 2217163DOI: 10.1002/prot.340080108 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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