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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 DOI10.2210/pdb1cbs/pdb
DescriptorCELLULAR RETINOIC ACID BINDING PROTEIN TYPE II, RETINOIC ACID (3 entities in total)
Functional Keywordsretinoic-acid transport
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight15882.24
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 citationKleywegt, 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: 7704533
DOI: 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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