Crystal Packing Analysis of Rhodopsin Crystals

Journal Article · Tue Jul 10 04:00:00 EDT 2007 · J.Struc.Biol.158:455,2007

DOI:https://doi.org/10.1016/j.jsb.2007.01.017· OSTI ID:909779

Lodowski, D T; Salom, D; Trong, I Le; Teller, D C; Ballesteros, J A; Palczewski, K; Stenkamp, R E

Oligomerization has been proposed as one of several mechanisms to regulate the activity of G protein-coupled receptors (GPCRs), but little is known about the structure of GPCR oligomers. Crystallographic analyses of two new crystal forms of rhodopsin reveal an interaction surface which may be involved in the formation of functional dimers or oligomers. New crystallization conditions lead to the formation of two crystal forms with similar rhodopsin-rhodopsin interactions, but changes in the crystal lattice are induced by the addition of different surfactant additives. However, the intermolecular interactions between rhodopsin molecules in these crystal structures may reflect the contacts necessary for the maintenance of dimers or oligomers in rod outer segment membranes. Similar contacts may assist in the formation of dimers or oligomers in other GPCRs as well. These new dimers are compared with other models proposed by crystallography or EM and AFM studies. The inter-monomer surface contacts are different for each model, but several of these models coincide in implicating helix I, II, and H-8 as contributors to the main contact surface stabilizing the dimers.

• Research Organization: Stanford Linear Accelerator Center (SLAC)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC02-76SF00515
• OSTI ID: 909779
• Report Number(s): SLAC-REPRINT-2007-115
• Journal Information: J.Struc.Biol.158:455,2007, Journal Name: J.Struc.Biol.158:455,2007 Vol. 158; ISSN JSBIEM; ISSN 1047-8477
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
ADDITIVES
CRYSTAL LATTICES
CRYSTAL STRUCTURE
CRYSTALLIZATION
CRYSTALLOGRAPHY
DIMERS
FUNCTIONALS
MAINTENANCE
MEMBRANES
Other
OTHER
RHODOPSIN
SURFACTANTS