Conformational activation of visual rhodopsin in native disc membranes-Reference-Cited by-同舟云学术

Conformational activation of visual rhodopsin in native disc membranes

Published:2015-03-10 Issue:367 Volume:8 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Malmerberg Erik¹,M. Bovee-Geurts Petra H.²,Katona Gergely¹,Deupi Xavier³⁴,Arnlund David¹,Wickstrand Cecilia¹,Johansson Linda C.¹,Westenhoff Sebastian¹,Nazarenko Elena¹,X. Schertler Gebhard F.⁴⁵,Menzel Andreas⁶,de Grip Willem J.²,Neutze Richard¹

Affiliation:

1. Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, 40530 Gothenburg, Sweden.

2. Department of Biochemistry, Radboud University Medical Center, P.O. Box 9101, 6500 HB Nijmegen, Netherlands.

3. Condensed Matter Theory Group, Paul Scherrer Institute, CH-5232 Villigen, Switzerland.

4. Laboratory of Biomolecular Research, Paul Scherrer Institute, CH-5232 Villigen, Switzerland.

5. Department of Biology, ETH Zürich, Wolfgang-Pauli-Str. 27, 8093 Zürich, Switzerland.

6. Swiss Light Source, Paul Scherrer Institute, CH-5232 Villigen, Switzerland.

Abstract

Structural analysis with TR-WAXS reveals a light-activated conformational change in rhodopsin in native membranes.

Funder

Swedish Research Council (Vetenskapsradet)

Swedish Strategic Research Foundation

Knut and Alice Wallenberg Foundation

Swiss National Science Foundation

COST Action

Femtosecond and Attosecond Science and Technology Initiative (ETH-FAST)

Marie Curie Initial Training Network NanoMem

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference64 articles.

1. The G-Protein-Coupled Receptors in the Human Genome Form Five Main Families. Phylogenetic Analysis, Paralogon Groups, and Fingerprints

2. Structure and Activation of the Visual Pigment Rhodopsin

3. Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

4. Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin

5. High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

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