Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid.Kleywegt, G.J., Bergfors, T., Senn, H., Le Motte, P., Gsell, B., Shudo, K., Jones, T.A.
(1994) Structure 2: 1241-1258
- PubMed: 7704533
- Primary Citation of Related Structures:
- PubMed Abstract:
- Crystallographic Studies on a Family of Lipophilic Transport Proteins. Refinement of P2 Myelin Protein and the Structure Determination and Refinement of Cellular Retinol-Binding Protein in Complex with All-Trans-Retinol
Cowan, S.W.,Newcomer, M.E.,Jones, T.A.
(1993) J.Mol.Biol. 230: 1225
- The Three-Dimensional Structure of P2 Myelin Protein
Jones, T.A.,Bergfors, T.,Sedzik, J.,Unge, T.
(1988) Embo J. 7: 1597
- Lipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Banaszak, L.,Winter, N.,Xu, Z.,Bernlohr, D.A.,Cowan, S.W.,Jones, T.A.
(1994) Adv.Protein Chem. 45: 89
- Crystallisation and Preliminary X-Ray Analysis of Recombinant Bovine Cellular Retinoic Acid-Binding Protein
Bergfors, T.,Kleywegt, G.J.,Jones, T.A.
(1994) Acta Crystallogr.,Sect.D 50: 370
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 ...
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.
Department of Molecular Biology, Uppsala University, Sweden.