1l9h

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[[Image:1l9h.gif|left|200px]]<br /><applet load="1l9h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l9h.gif|left|200px]]
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caption="1l9h, resolution 2.6&Aring;" />
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'''Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION'''<br />
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{{Structure
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|PDB= 1l9h |SIZE=350|CAPTION= <scene name='initialview01'>1l9h</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene> and <scene name='pdbligand=RET:RETINAL'>RET</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1L9H is a [[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=1L9H OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11972040 11972040]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11972040 11972040]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: retinal protein]]
[[Category: retinal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:11 2008''

Revision as of 10:28, 20 March 2008

Image:1l9h.gif


PDB ID 1l9h

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands: , , , , , and
Coordinates: save as pdb, mmCIF, xml



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. 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

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