1CBS
CRYSTAL STRUCTURE OF CELLULAR RETINOIC-ACID-BINDING PROTEINS I AND II IN COMPLEX WITH ALL-TRANS-RETINOIC ACID AND A SYNTHETIC RETINOID
Summary for 1CBS
Entry DOI | 10.2210/pdb1cbs/pdb |
Descriptor | CELLULAR RETINOIC ACID BINDING PROTEIN TYPE II, RETINOIC ACID (3 entities in total) |
Functional Keywords | retinoic-acid transport |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 15882.24 |
Authors | Kleywegt, G.J.,Bergfors, T.,Jones, T.A. (deposition date: 1994-09-28, release date: 1995-01-26, Last modification date: 2024-02-07) |
Primary citation | Kleywegt, G.J.,Bergfors, T.,Senn, H.,Le Motte, P.,Gsell, B.,Shudo, K.,Jones, T.A. Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure, 2:1241-1258, 1994 Cited by PubMed Abstract: Retinoic acid (RA) plays a fundamental role in diverse cellular activities. Cellular RA binding proteins (CRABPs) are thought to act by modulating the amount of RA available to nuclear RA receptors. CRABPs and cellular retinol-binding proteins (CRBPs) share a unique fold of two orthogonal beta-sheets that encapsulate their ligands. It has been suggested that a trio of residues are the prime determinants defining the high specificity of CRBPs and CRABPs for their physiological ligands. PubMed: 7704533DOI: 10.1016/S0969-2126(94)00125-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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