1FD0

ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254

Summary for 1FD0

• Entry DOI: 10.2210/pdb1fd0/pdb
• Related: 1EXA 1EXX 1fcx 1fcy 1fcz 2LBD 3LBD
• Descriptor: RETINOIC ACID RECEPTOR GAMMA-1, 6-[HYDROXYIMINO-(5,5,8,8-TETRAMETHYL-5,6,7,8-TETRAHYDRO-NAPHTALEN-2-YL)-METHYL]-NAPHTALENE-2-CARBOXYLIC ACID, DODECYL-ALPHA-D-MALTOSIDE, ... (4 entities in total)
• Functional Keywords: isotype selectivity, retinoid ligand complexes, drug design, antiparallel alpha-helical sandwich fold, ch...o hydrogen bond, structural proteomics in europe, spine, structural genomics, gene regulation
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 27447.18

Authors

Klaholz, B.P.,Moras, D.,Structural Proteomics in Europe (SPINE) (deposition date: 2000-07-19, release date: 2002-09-27, Last modification date: 2023-08-09)

Primary citation

Klaholz, B.,Moras, D.
C-H...O hydrogen bonds in the nuclear receptor RARgamma--a potential tool for drug selectivity.
Structure, 10:1197-1204, 2002

PubMed Abstract: Hydrogen bonds between polarized atoms play a crucial role in protein interactions and are often used in drug design, which usually neglects the potential of C-H...O hydrogen bonds. The 1.4 A resolution crystal structure of the ligand binding domain of the retinoic acid receptor RARgamma complexed with the retinoid SR11254 reveals several types of C-H...O hydrogen bonds. A striking example is the hydroxyl group of the ligand that acts as an H bond donor and acceptor, leading to a synergy between classical and C-H...O hydrogen bonds. This interaction introduces both specificity and affinity within the hydrophobic ligand pocket. The similarity of intraprotein and protein-ligand C-H...O interactions suggests that such bonds should be considered in rational drug design approaches.

PubMed: 12220491
DOI: 10.1016/S0969-2126(02)00828-6

Experimental method

X-RAY DIFFRACTION (1.38 Å)