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Structural changes of a light-activa...

Crocker, Evan Daniel.

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Structural changes of a light-activated G protein-coupled receptor determined by solid-state NMR: Channeling light energy into the visual pigment rhodopsin.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Structural changes of a light-activated G protein-coupled receptor determined by solid-state NMR: Channeling light energy into the visual pigment rhodopsin./
作者:	Crocker, Evan Daniel.
面頁冊數:	122 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-06, Section: B, page: 3200.
Contained By:	Dissertation Abstracts International66-06B.
標題:	Physics, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3179625
ISBN:	0542201836

Structural changes of a light-activated G protein-coupled receptor determined by solid-state NMR: Channeling light energy into the visual pigment rhodopsin.
Crocker, Evan Daniel.

Structural changes of a light-activated G protein-coupled receptor determined by solid-state NMR: Channeling light energy into the visual pigment rhodopsin. - 122 p.

Source: Dissertation Abstracts International, Volume: 66-06, Section: B, page: 3200.

Thesis (Ph.D.)--State University of New York at Stony Brook, 2005.

Absorption of light by the visual pigment rhodopsin triggers an 11- cis to all-trans isomerization of the retinal chromophore within the interior of this G protein-coupled receptor. Two-dimensional solid-state NMR of rhodopsin and the active metarhodopsin II intermediate is used to determine the trajectory of the retinal and the effects of retinal isomerization on the structure of the protein.

ISBN: 0542201836Subjects--Topical Terms:

1018648
Physics, Molecular.

Structural changes of a light-activated G protein-coupled receptor determined by solid-state NMR: Channeling light energy into the visual pigment rhodopsin.
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245 1 0 $a Structural changes of a light-activated G protein-coupled receptor determined by solid-state NMR: Channeling light energy into the visual pigment rhodopsin.
300 $a 122 p.
500 $a Source: Dissertation Abstracts International, Volume: 66-06, Section: B, page: 3200.
500 $a Adviser: Steven O. Smith.
502 $a Thesis (Ph.D.)--State University of New York at Stony Brook, 2005.
520 $a Absorption of light by the visual pigment rhodopsin triggers an 11- cis to all-trans isomerization of the retinal chromophore within the interior of this G protein-coupled receptor. Two-dimensional solid-state NMR of rhodopsin and the active metarhodopsin II intermediate is used to determine the trajectory of the retinal and the effects of retinal isomerization on the structure of the protein.
520 $a Structural constraints obtained in this study indicate that helices H5, H6 and H7 undergo changes in orientation relative to the H1--H4 core of the receptor upon retinal isomerization. The position of the retinal beta-ionone ring in metarhodopsin II was found to translate toward and interact with H5. Changes observed in the H4--H5 interface are consistent with a small counter clockwise rotation of H5, as observed from the extracellular side of the protein.
520 $a Retinal isomerization also alters the structure and position of H6. The position of Trp265 relative to H3 and the retinal in metarhodopsin II indicates that the extracellular end of H6 moves inward and rotates upon activation. Together with previous EPR measurements of the relative positions of the intracellular ends of H3 and H6 in metarhodopsin II, the NMR constraints define how Trp265 serves as a lever for the motion of H6.
520 $a Retinal translation also leads to an inward motion of the extracellular end of H7, suggesting that H6 and H7 move in concert upon receptor activation. A function of the highly conserved NPxxY sequence on the intracellular end of H7 is proposed.
520 $a Based on the observations described above and indications that helices H1 through H4 form a stable core that serves as a platform for the motion of H5, H6 and H7, a model for the structure of the active state of rhodopsin is presented. Aspects of this model are put into the context of the proposed activation mechanisms of other members of the GPCR superfamily.
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791 $a Ph.D.
792 $a 2005
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