1l9h
From Proteopedia
(New page: 200px<br /><applet load="1l9h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l9h, resolution 2.6Å" /> '''Crystal structure of ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1l9h.gif|left|200px]]<br /><applet load="1l9h" size=" | + | [[Image:1l9h.gif|left|200px]]<br /><applet load="1l9h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l9h, resolution 2.6Å" /> | caption="1l9h, resolution 2.6Å" /> | ||
'''Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION'''<br /> | '''Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Activation of G protein-coupled receptors (GPCRs) is triggered and | + | Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs. Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 A. The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively. To confirm the physiological relevance of the structural findings, we conducted single-crystal microspectrophotometry on rhodopsin packed in our three-dimensional crystals and show that its spectroscopic properties are similar to those previously found by using bovine rhodopsin in suspension or membrane environment. |
==About this Structure== | ==About this Structure== | ||
| - | 1L9H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with BNG, HG, ZN, ACE, HTO, PLM and RET as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1L9H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=BNG:'>BNG</scene>, <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=HTO:'>HTO</scene>, <scene name='pdbligand=PLM:'>PLM</scene> and <scene name='pdbligand=RET:'>RET</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9H OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fujiyoshi, Y.]] | [[Category: Fujiyoshi, Y.]] | ||
| - | [[Category: Landau, E | + | [[Category: Landau, E M.]] |
[[Category: Navarro, J.]] | [[Category: Navarro, J.]] | ||
[[Category: Okada, T.]] | [[Category: Okada, T.]] | ||
| Line 31: | Line 31: | ||
[[Category: retinal protein]] | [[Category: retinal protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:49 2008'' |
Revision as of 11:42, 21 February 2008
|
Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION
Overview
Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs. Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 A. The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively. To confirm the physiological relevance of the structural findings, we conducted single-crystal microspectrophotometry on rhodopsin packed in our three-dimensional crystals and show that its spectroscopic properties are similar to those previously found by using bovine rhodopsin in suspension or membrane environment.
About this Structure
1L9H is a Single protein structure of sequence from Bos taurus with , , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography., Okada T, Fujiyoshi Y, Silow M, Navarro J, Landau EM, Shichida Y, Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5982-7. Epub 2002 Apr 23. PMID:11972040
Page seeded by OCA on Thu Feb 21 13:42:49 2008
Categories: Bos taurus | Single protein | Fujiyoshi, Y. | Landau, E M. | Navarro, J. | Okada, T. | Shichida, Y. | Silow, M. | ACE | BNG | HG | HTO | PLM | RET | ZN | G protein-coupled receptor | Membrane protein | Photoreceptor | Retinal protein
