Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2CBS

CELLULAR RETINOIC ACID BINDING PROTEIN II IN COMPLEX WITH A SYNTHETIC RETINOIC ACID (RO-13 6307)

Summary for 2CBS
Entry DOI10.2210/pdb2cbs/pdb
DescriptorPROTEIN (CRABP-II), 3-METHYL-7-(5,5,8,8-TETRAMETHYL-5,6,7,8-TETRAHYDRO-NAPHTHALEN-2-YL) -OCTA-2,4,6-TRIENOIC ACID (3 entities in total)
Functional Keywordsretinoic-acid transport, transport protein
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight15920.28
Authors
Chaudhuri, B.,Kleywegt, G.J.,Bergfors, T.,Jones, T.A. (deposition date: 1999-02-22, release date: 1999-12-22, Last modification date: 2023-08-23)
Primary citationChaudhuri, B.N.,Kleywegt, G.J.,Broutin-L'Hermite, I.,Bergfors, T.,Senn, H.,Le Motte, P.,Partouche, O.,Jones, T.A.
Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids.
Acta Crystallogr.,Sect.D, 55:1850-1857, 1999
Cited by
PubMed Abstract: Retinoids play important roles in diverse cellular processes including growth, cell differentiation and vision. Many natural and synthetic retinoids are used as drugs in dermatology and oncology. A large amount of data has been accumulated on the cellular activity of different synthetic retinoids. They are stabilized and transported inside the cell cytoplasm by binding and transport proteins, such as cellular retinol-binding proteins and cellular retinoic acid binding proteins (CRABPs). The structures of human CRABP II in complex with two different synthetic retinoids, Ro13-6307 and Ro12--7310 (at 2.1 and 2.0 A resolution, respectively) and of bovine CRABP I in complex with a retinobenzoic acid, Am80 (at 2.8 A resolution) are described. The binding affinities of human CRABP I and II for the retinoids studied here have been determined. All these compounds have comparable binding affinities (nanomolar range) for both CRABPs. Apart from the particular interactions of the carboxylate group of the retinoids with specific protein groups, each structure reveals characteristic interactions. Studying the atomic details of the interaction of retinoids with retinoid-binding proteins facilitates the understanding of the kinetics of retinoid trafficking inside the cytoplasm.
PubMed: 10531482
DOI: 10.1107/S0907444999011026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon