PDBsum entry 2cbs

Transport protein

PDB id: 2cbs

Contents

Protein chain

137 a.a. *

Ligands

R13

Waters ×53

* Residue conservation analysis

PDB id:

2cbs

Name:

Transport protein

Title:

Cellular retinoic acid binding protein ii in complex with a synthetic retinoic acid (ro-13 6307)

Structure:

Protein (crabp-ii). Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytoplasm. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.10Å R-factor: 0.200 R-free: 0.233

Authors:

B.Chaudhuri,G.J.Kleywegt,T.Bergfors,T.A.Jones

Key ref:

B.N.Chaudhuri et al. (1999). Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids. Acta Crystallogr D Biol Crystallogr, 55, 1850-1857. PubMed id: 10531482 DOI: 10.1107/S0907444999011026

Date:

22-Feb-99 Release date: 22-Dec-99

Protein chain

P29373  (RABP2_HUMAN) -  Cellular retinoic acid-binding protein 2 from Homo sapiens

Seq: 138 a.a.

Struc: 137 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S0907444999011026

Acta Crystallogr D Biol Crystallogr 55:1850-1857 (1999)

PubMed id: 10531482

Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids.

B.N.Chaudhuri, G.J.Kleywegt, I.Broutin-L'Hermite, T.Bergfors, H.Senn, P.Le Motte, O.Partouche, T.A.Jones.

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.

Selected figure(s)

Figure 1.
Figure 1 C^ trace of CRABP II in complex with retinoic acid (PDB code 1cbs).

Figure 6.
Figure 6 The interaction of Am80 with CRABP I (yellow C atoms; red O atoms; blue N atoms). [A]-weighted simulated-annealing omit density for the ligand (Read, 1986[Read, R. J. (1986). Acta Cryst. A42, 140-149.]; Hodel et al., 1992[Hodel, A., Kim, S.-H. & Brünger, A. T. (1992). Acta Cryst. A48, 851-858.]) is shown. Hydrogen-bonding interactions are indicated by dashed lines.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1850-1857) copyright 1999.

Figures were selected by the author.