A structural model for the chromophore-binding domain of ovine rhodopsin

Eliopoulos, Elias; Geddes, A. J.; Brett, M.; Pappin, Darryl; Findlay, John B. C.

doi:10.1016/0141-8130(82)90053-8

Cited by 67 publications

(35 citation statements)

References 25 publications

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“…#16 refers to $ calculated over a 16 residue length of sequence which shows the most amphipathicity. Values of & and $16 which are greater than 2 reflect a high probability of an amphipathic helix over the length of the sequence used the retinal binding domain [2,3,7]. The equivalent position to the retinal binding lysine of bovine opsin in our alignment is the Y-407 in the human Ml subtype of the muscarinic cholinergic receptor.…”

Section: Resultsmentioning

confidence: 99%

An analysis of the periodicity of conserved residues in sequence alignments of G‐protein coupled receptors

et al. 1989

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Twenty-three sequences from the family of G-protein coupled receptors have been aligned according to the 'historical alignment' procedure of Feng and Doolittle. Fourier transform analysis of this reveals that parts of five of the seven putative membrane-spanning regions exhibit a periodicity of conserved/nonconserved residues which is compatible with the periodicity of the a-helix. This would place the conserved residues on one side of the helix, which may face the inside of the proposed seven membered helical bundle.

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Section: Resultsmentioning

confidence: 99%

An analysis of the periodicity of conserved residues in sequence alignments of G‐protein coupled receptors

et al. 1989

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“…Secondary structure prediction from the amino acid sequence (Lee et al, 1991) was made using the Leeds package of algorithms (Eliopoulos et al, 1982). Regions of sequence identity and homology were identified by comparisons of the amino acid sequence of L. mesenteroides G6PD with those of G6PDs from human (Persico et al, 1986), rat (Ho et al, 1988), Drosophila (Fouts et al, 1988), Saccharomyces cerevisiae (Nogae & Johnston, 1990;Thomas et al, 1991), E. coli (Rowley & Wolf, 1991), and Zymomonas mobilis (Barnell et al, 1990), using a multiple sequence alignment and prediction protocol (Russell et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

Site‐directed mutagenesis to facilitate X‐ray structural studies of leuconostoc mesenteroides glucose 6‐phosphate dehydrogenase

et al. 1993

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“…Secondary structure predictions using the joint prediction algorithm [25], together with hydrophobic moment analysis and surface profile prediction (from residue hydrophilicity, flexibility and accessibility parameters), enabled us roughly to define the eight putative P-strands (A -H) of crustacyanin A2 forming the P-barrel: A (31-39), B (42-49), C (58-67), D (72-81), E(84-94), F (97-108), G (112-122) and H (128-135). In the sequence alignment with RBP several of the residues in contact with retinol [I21 were found to be conserved in crustacyanin A2.…”

Section: Consensus Imentioning

confidence: 99%

Complete sequence and model for the A₂ subunit of the carotenoid pigment complex, crustacyanin

Keen

Caceres

Eliopoulos

et al. 1991

European Journal of Biochemistry

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The complete sequence has been determined for the A2 subunit of crustacyanin, an astaxanthin-binding protein from the carapace of the lobster Homarus gammarus. The polypeptide chain is 174 residues long and is similar to proteins of the retinol-binding protein superfamily. Some regions of the sequence are most similar to the retinolbinding protein, P-lactoglobulin subgroup, while the disulphide bonding pattern is more akin to that seen in the porphyrin binding proteins insecticyanin and bilin-binding protein. It is beginning to appear as though this superfamily of proteins, characterized by a similar gross structural framework, may be further subdivided into interrelated subclasses. Model building based on the coordinates of the known structure of human plasma retinolbinding protein and on empirical prediction algorithms has allowed the putative identification of side-chains which line the binding cavity. This pocket is larger than in retinol binding protein and P-lactoglobulin but does not allow the carotenoid to adopt a folded conformation. The amino acid composition of the pocket does not support a 'charge-shift'-type hypothesis to support the bathochromic shift phenomenon which takes place on interaction of the chromophore with the protein. Instead aromatic side-chains may play a prominent role.The blue colouration of the carapace of the lobster Homarus gammarus (L.) is provided by the astaxanthin (3,3'-dihydroxy-P,P-carotene-4,4'-dione) binding protein, acrustacyanin. Early interest in the carotenoprotein stemmed from similarities in its absorption characteristics to the visual pigment, rhodopsin [I]. Like rhodopsin, the absorption spectrum of the carotenoid (, , , 478 nm in acetone) is bathochromically shifted, without alteration in shape, by some 150 nm in the carotenoid-protein complex. Carotenoproteins occur ubiquitously in invertebrates where they may colour variously (red, purple, blue or green) eggs, ovary, blood or external surface (reviewed [2] and [3]).The physical and chemical properties of crustacyanin have been studied by a number of workers [4-91. The native pigment, a-crustacyanin, of molecular mass about 350 kDa is an aggregate of I6 apoprotein units of about 20 kDa, one astaxanthin molecule being bound/apoprotein monomer. The apoprotein consists of five electrophoretically distinct components which, from amino acid composition, size estimation and peptide mapping, fall into two main types: C1, Cz and Al (type I) and A2 and A3 (type 11), with C1 and Az predominating. Dimerization to form purple P-crustacyanin, also present in the lobster carapace, is brought about by association of two apoproteins, one of each type, with two carotenoid molecules; eight P-crustacyanin-sized units then associate to form a-crustacyanin. Correspondence to J . B. C . Findlay, Department of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, EnglandAbbreviations. RBP, retinol-binding protein; Pth-Xaa, phenylthiohydantoin derivative of amino acid Xaa; Hyd, Aro, Bas and Acd, hydrophobic, aromatic...

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A structural model for the chromophore-binding domain of ovine rhodopsin

Cited by 67 publications

References 25 publications

An analysis of the periodicity of conserved residues in sequence alignments of G‐protein coupled receptors

An analysis of the periodicity of conserved residues in sequence alignments of G‐protein coupled receptors

Site‐directed mutagenesis to facilitate X‐ray structural studies of leuconostoc mesenteroides glucose 6‐phosphate dehydrogenase

Complete sequence and model for the A₂ subunit of the carotenoid pigment complex, crustacyanin

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A structural model for the chromophore-binding domain of ovine rhodopsin

Cited by 67 publications

References 25 publications

An analysis of the periodicity of conserved residues in sequence alignments of G‐protein coupled receptors

An analysis of the periodicity of conserved residues in sequence alignments of G‐protein coupled receptors

Site‐directed mutagenesis to facilitate X‐ray structural studies of leuconostoc mesenteroides glucose 6‐phosphate dehydrogenase

Complete sequence and model for the A2 subunit of the carotenoid pigment complex, crustacyanin

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Complete sequence and model for the A₂ subunit of the carotenoid pigment complex, crustacyanin