1ayr
From Proteopedia
(New page: 200px<br /><applet load="1ayr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ayr, resolution 3.3Å" /> '''ARRESTIN FROM BOVINE ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ayr.jpg|left|200px]]<br /><applet load="1ayr" size=" | + | [[Image:1ayr.jpg|left|200px]]<br /><applet load="1ayr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ayr, resolution 3.3Å" /> | caption="1ayr, resolution 3.3Å" /> | ||
'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''<br /> | '''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Retinal arrestin is the essential protein for the termination of the light | + | Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 A resolution. The crystal structure comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin. |
==About this Structure== | ==About this Structure== | ||
| - | 1AYR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1AYR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYR OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bueldt, G.]] | [[Category: Bueldt, G.]] | ||
| - | [[Category: Choe, H | + | [[Category: Choe, H W.]] |
[[Category: Granzin, J.]] | [[Category: Granzin, J.]] | ||
[[Category: Krafft, B.]] | [[Category: Krafft, B.]] | ||
| Line 23: | Line 23: | ||
[[Category: sensory transduction]] | [[Category: sensory transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:42 2008'' |
Revision as of 09:49, 21 February 2008
|
ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
Overview
Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 A resolution. The crystal structure comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin.
About this Structure
1AYR is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of arrestin from bovine rod outer segments., Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Buldt G, Nature. 1998 Feb 26;391(6670):918-21. PMID:9495348
Page seeded by OCA on Thu Feb 21 11:49:42 2008
