Rhodopsin helix-helix interactions found experimentally.
Residue Indices | Experimental Methods | Residues/Mutations | Cβ-Cβ | References | |||||
---|---|---|---|---|---|---|---|---|---|
C | R | Z | E | L | F | ||||
Å | |||||||||
1.60 7.63 | + | + | H65C C316 | 5.3 | Yang et al., 1996; Struthers et al., 2000 | ||||
2.57 7.43 | + | G90D K296 | 8.31-a | Oprian, 1992; Rao et al., 1994 | |||||
3.28 7.43 | + | E113 K296 | 10.1 | Oprian, 1992; Rao et al., 1994 | |||||
3.36 5.22 | + | C110 C187 | 12.9 | Struthers et al., 2000 | |||||
3.36 6.44 | + | G121L F261A | 9.0 | Han et al., 1996; Lin et al., 2000 | |||||
3.37 5.46 | + | E122 H211 | 6.1 | Beck et al., 1998 | |||||
3.51 5.57 | + | Y136C C222 | 5.1 | Yu and Oprian, 1999 | |||||
3.51 5.60 | + | Y136C C225 | 6.0 | Yu and Oprian, 1999 | |||||
3.53 6.34 | + | V138H T251H | 8.3 | Sheikh et al., 1996 | |||||
3.54 5.60 | + | V139C Q225C | 8.6 | Yu and Oprian, 1999 | |||||
3.54 6.30 | + | V139C E247C | 6.3 | Farrens et al., 1996 | |||||
3.54 6.31 | + | + | V139C K248C | 8.2 | Farrens et al., 1996 | ||||
3.54 6.32 | + | + | V139C E249C | 11.8 | Farrens et al., 1996 | ||||
3.54 6.33 | + | + | V139C V250C | 8.9 | Farrens et al., 1996 | ||||
3.54 6.34 | + | + | V139C T251C | 5.7 | Farrens et al., 1996 | ||||
3.54 6.35 | + | V139C R252C | 10.8 | Farrens et al., 1996 | |||||
3.55 5.57 | + | C140 C222 | 8.3 | Farrens et al., 1996; Yu and Oprian, 1999 | |||||
3.55 5.60 | + | C140 Q225C | 4.9 | Yu and Oprian, 1999; Struthers et al., 2000 | |||||
3.55 7.63 | + | C140 C316 | 28.51-a | Yu et al., 1999 | |||||
5.33 6.59 | + | T198C F276C | 14.5 | Struthers et al., 1999 | |||||
5.35 6.59 | + | N200C F276C | 9.0 | Struthers et al., 1999 | |||||
5.39 6.59 | + | V204C F276C | 5.1 | 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.