Table 1

Rhodopsin helix-helix interactions found experimentally.

Residue IndicesExperimental MethodsResidues/MutationsCβ-CβReferences
CRZELF
Å
1.60 7.63 + + H65C C3165.3 Yang et al., 1996; Struthers et al., 2000
2.57 7.43 + G90D K2968.31-a Oprian, 1992; Rao et al., 1994
3.28 7.43 + E113 K29610.1 Oprian, 1992; Rao et al., 1994
3.36 5.22 + C110 C18712.9 Struthers et al., 2000
3.36 6.44 + G121L F261A9.0 Han et al., 1996; Lin et al., 2000
3.37 5.46 + E122 H2116.1 Beck et al., 1998
3.51 5.57 + Y136C C2225.1 Yu and Oprian, 1999
3.51 5.60 + Y136C C2256.0 Yu and Oprian, 1999
3.53 6.34 + V138H T251H8.3 Sheikh et al., 1996
3.54 5.60 + V139C Q225C8.6 Yu and Oprian, 1999
3.54 6.30 + V139C E247C6.3 Farrens et al., 1996
3.54 6.31 + + V139C K248C8.2 Farrens et al., 1996
3.54 6.32 + + V139C E249C11.8 Farrens et al., 1996
3.54 6.33 + + V139C V250C8.9 Farrens et al., 1996
3.54 6.34 + + V139C T251C5.7 Farrens et al., 1996
3.54 6.35 + V139C R252C10.8 Farrens et al., 1996
3.55 5.57 + C140 C2228.3 Farrens et al., 1996; Yu and Oprian, 1999
3.55 5.60 + C140 Q225C4.9 Yu and Oprian, 1999; Struthers et al., 2000
3.55 7.63 + C140 C31628.51-a Yu et al., 1999
5.33 6.59 + T198C F276C14.5 Struthers et al., 1999
5.35 6.59 + N200C F276C9.0 Struthers et al., 1999
5.39 6.59 + V204C F276C5.1 Struthers et al., 1999, 2000

Cβ-Cβ is the distance between the Cβ of two residues in the bovine rhodopsin structure. Receptor names are abbreviated according to their SWISS-PROT Annotated Protein Sequence Database entry names:http://www.expasy.ch/cgi-bin/lists?7trmrlist.txt

    • C, Cys-Cys crosslinking; R, double revertant mutations; Z, Zinc-His binding; E, spin-labeling; L, ligand related; F, Fourier-transform infrared difference spectroscopy.

    • 1-a  Present only in the active state.