Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 26 November 1993:
Vol. 262. no. 5138, pp. 1416 - 1419
DOI: 10.1126/science.8248781
Prev | Table of Contents | Next

Articles

Science, Vol 262, Issue 5138, 1416-1419
Copyright © 1993 by American Association for the Advancement of Science

articles

Photoactivated conformational changes in rhodopsin: a time-resolved spin label study

ZT Farahbakhsh, K Hideg, and WL Hubbell

Jules Stein Eye Institute, Los Angeles, CA.

Rhodopsin has been selectively spin-labeled near the cytoplasmic termini of helices C and G. Photoactivation with a light flash induces an electron paramagnetic resonance spectral change in the millisecond time domain, coincident with the appearance of the active metarhodopsin II intermediate. The spectral change is consistent with a small movement near the cytoplasmic termination of the C helix and reverses upon formation of the MIII state. These results provide an important link between the optical changes associated with the retinal chromophore and protein conformational states.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Sequence of late molecular events in the activation of rhodopsin.
B. Knierim, K. P. Hofmann, O. P. Ernst, and W. L. Hubbell (2007)
PNAS 104, 20290-20295
   Abstract »    Full Text »    PDF »
Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein {alpha}-Subunit: NMR ANALYSIS OF GTP{gamma}S-BOUND STATES.
K. D. Ridge, N. G. Abdulaev, C. Zhang, T. Ngo, D. M. Brabazon, and J. P. Marino (2006)
J. Biol. Chem. 281, 7635-7648
   Abstract »    Full Text »    PDF »
Equilibrium between Metarhodopsin-I and Metarhodopsin-II Is Dependent on the Conformation of the Third Cytoplasmic Loop.
C. L. Piscitelli, T. E. Angel, B. W. Bailey, P. Hargrave, E. A. Dratz, and C. M. Lawrence (2006)
J. Biol. Chem. 281, 6813-6825
   Abstract »    Full Text »    PDF »
Partial Agonism in a G Protein-coupled Receptor: ROLE OF THE RETINAL RING STRUCTURE IN RHODOPSIN ACTIVATION.
F. J. Bartl, O. Fritze, E. Ritter, R. Herrmann, V. Kuksa, K. Palczewski, K. P. Hofmann, and O. P. Ernst (2005)
J. Biol. Chem. 280, 34259-34267
   Abstract »    Full Text »    PDF »
Synergistic Contributions of the Functional Groups of Epinephrine to Its Affinity and Efficacy at the {beta}2 Adrenergic Receptor.
G. Liapakis, W. C. Chan, M. Papadokostaki, and J. A. Javitch (2004)
Mol. Pharmacol. 65, 1181-1190
   Abstract »    Full Text »
Rhodopsin: Structural Basis of Molecular Physiology.
S. T. Menon, M. Han, and T. P. Sakmar (2001)
Physiol Rev 81, 1659-1688
   Abstract »    Full Text »    PDF »
Functional Segregation of the Highly Conserved Basic Motifs within the Third Endoloop of the Human Secretin Receptor.
K. Y.-Y. Chan, R. T.-K. Pang, and B. K.-C. Chow (2001)
Endocrinology 142, 3926-3934
   Abstract »    Full Text »    PDF »
Differences in conformational properties of the second intracellular loop (IL2) in 5HT2C receptors modified by RNA editing can account for G protein coupling efficiency.
I. Visiers, S. A. Hassan, and H. Weinstein (2001)
Protein Eng. Des. Sel. 14, 409-414
   Abstract »    Full Text »    PDF »
Solution 19F nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin.
M. C. Loewen, J. Klein-Seetharaman, E. V. Getmanova, P. J. Reeves, H. Schwalbe, and H. G. Khorana (2001)
PNAS 98, 4888-4892
   Abstract »    Full Text »    PDF »
Adaptation in Vertebrate Photoreceptors.
G. L. Fain, H. R. Matthews, M. C. Cornwall, and Y. Koutalos (2001)
Physiol Rev 81, 117-151
   Abstract »    Full Text »    PDF »
Uncovering Molecular Mechanisms Involved in Activation of G Protein-Coupled Receptors.
U. Gether (2000)
Endocr. Rev. 21, 90-113
   Abstract »    Full Text »
Use of a Disulfide Cross-linking Strategy to Study Muscarinic Receptor Structure and Mechanisms of Activation.
F.-Y. Zeng, A. Hopp, A. Soldner, and J. Wess (1999)
J. Biol. Chem. 274, 16629-16640
   Abstract »    Full Text »    PDF »
C5a Receptor Activation. GENETIC IDENTIFICATION OF CRITICAL RESIDUES IN FOUR TRANSMEMBRANE HELICES.
T. J. Baranski, P. Herzmark, O. Lichtarge, B. O. Gerber, J. Trueheart, E. C. Meng, T. Iiri, S. P. Sheikh, and H. R. Bourne (1999)
J. Biol. Chem. 274, 15757-15765
   Abstract »    Full Text »    PDF »
Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin.
N. G. Abdulaev and K. D. Ridge (1998)
PNAS 95, 12854-12859
   Abstract »    Full Text »    PDF »
G Protein-coupled Receptors. II. MECHANISM OF AGONIST ACTIVATION.
U. Gether and B. K. Kobilka (1998)
J. Biol. Chem. 273, 17979-17982
   Full Text »    PDF »
Antagonists of the Receptor-G Protein Interface Block Gi-coupled Signal Transduction.
A. Gilchrist, M. R. Mazzoni, B. Dineen, A. Dice, J. Linden, W. R. Proctor, C. R. Lupica, T. V. Dunwiddie, and H. E. Hamm (1998)
J. Biol. Chem. 273, 14912-14919
   Abstract »    Full Text »    PDF »
Mechanisms Governing the Activation and Trafficking of Yeast G Protein-coupled Receptors.
C. J. Stefan, M. C. Overton, and K. J. Blumer (1998)
Mol. Biol. Cell 9, 885-899
   Abstract »    Full Text »
Structure and function in rhodopsin: Topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops.
K. Cai, R. Langen, W. L. Hubbell, and H. G. Khorana (1997)
PNAS 94, 14267-14272
   Abstract »    Full Text »    PDF »
Structure and function in rhodopsin: Rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state.
J.-M. Kim, C. Altenbach, R. L. Thurmond, H. G. Khorana, and W. L. Hubbell (1997)
PNAS 94, 14273-14278
   Abstract »    Full Text »    PDF »
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
M. Han, M. Groesbeek, T. P. Sakmar, and S. O. Smith (1997)
PNAS 94, 13442-13447
   Abstract »    Full Text »    PDF »
Modulation of Opsin Apoprotein Activity by Retinal. DARK ACTIVITY OF RHODOPSIN FORMED AT LOW TEMPERATURE.
A. Surya and B. E. Knox (1997)
J. Biol. Chem. 272, 21745-21750
   Abstract »    Full Text »    PDF »
Chromophore structural changes in rhodopsin from nanoseconds to microseconds following pigment photolysis.
S. Jager, J. W. Lewis, T. A. Zvyaga, I. Szundi, T. P. Sakmar, and D. S. Kliger (1997)
PNAS 94, 8557-8562
   Abstract »    Full Text »    PDF »
Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin.
H. Steinhoff, R Mollaaghababa, C Altenbach, K Hideg, M Krebs, H. Khorana, and W. Hubbell (1994)
Science 266, 105-107
   Abstract »    PDF »
Functionally Different Agonists Induce Distinct Conformations in the G Protein Coupling Domain of the beta 2 Adrenergic Receptor.
P. Ghanouni, Z. Gryczynski, J. J. Steenhuis, T. W. Lee, D. L. Farrens, J. R. Lakowicz, and B. K. Kobilka (2001)
J. Biol. Chem. 276, 24433-24436
   Abstract »    Full Text »    PDF »
Agonist-induced Conformational Changes at the Cytoplasmic Side of Transmembrane Segment 6 in the beta 2 Adrenergic Receptor Mapped by Site-selective Fluorescent Labeling.
A. D. Jensen, F. Guarnieri, S. G. F. Rasmussen, F. Asmar, J. A. Ballesteros, and U. Gether (2001)
J. Biol. Chem. 276, 9279-9290
   Abstract »    Full Text »    PDF »
Functionally Discrete Mimics of Light-activated Rhodopsin Identified through Expression of Soluble Cytoplasmic Domains.
N. G. Abdulaev, T. Ngo, R. Chen, Z. Lu, and K. D. Ridge (2000)
J. Biol. Chem. 275, 39354-39363
   Abstract »    Full Text »    PDF »
Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor.
P. Ghanouni, J. J. Steenhuis, D. L. Farrens, and B. K. Kobilka (2001)
PNAS 98, 5997-6002
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)