1l9h: Difference between revisions

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[[Image:1l9h.gif|left|200px]]<br /><applet load="1l9h" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1l9h.gif|left|200px]]<br /><applet load="1l9h" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1l9h, resolution 2.6Å" />

'''Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1L9H OCA].

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==

Line 14:

[[Category: Single protein]]

[[Category: Fujiyoshi, Y.]]

[[Category: Landau, E.M.]]

[[Category: Landau, E M.]]

[[Category: Navarro, J.]]

[[Category: Okada, T.]]

Line 31:

[[Category: retinal protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:24:~~03 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:49 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1l9h.gif|left|200px]]<br /><applet load="1l9h" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1l9h.gif|left|200px]]<br /><applet load="1l9h" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1l9h, resolution 2.6&Aring;" />
 '''Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION'''<br />
 ==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.
+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==
-L9H 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L9H OCA].
+L9H 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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Fujiyoshi, Y.]]
-[[Category: Landau, E.M.]]
+[[Category: Landau, E M.]]
 [[Category: Navarro, J.]]
 [[Category: Okada, T.]]
@@ Line 31: / Line 31: @@
 [[Category: retinal protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:24:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:49 2008''