User:Anat Levit/Sandbox 1: Difference between revisions

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The ligand binding pocket of bovine Rhodopsin is similar in position to the β2-Adrenergic receptor binding site, and also involves TMs II, III, V and VI. The position does not vary considerably with alternate ligands or between different subtypes of different species. The retinal binding pocket relies mainly on hydrophobic interactions in addition to a covalent linkage with TM VII. In both, <scene name='User:Anat_Levit/Sandbox_1/Pkr1_1l9h_based_residues/3' target='PROKR1'>PROKR1</scene> and

<scene name='User:Anat_Levit/Sandbox_1/Pkr2_1l9h_residues/1' target='PROKR2'>PROKR2</scene>, Trp288 is part of the binding pocket. This position is homologues to Trp265 of Rhodopsin which interacts with retinal (a tryptophan is in general conserved at this position in class A receptors and is thought to be involved in receptor signaling).

<scene name='User:Anat_Levit/Sandbox_1/Pkr2_1l9h_residues/1' target='PROKR2'>PROKR2</scene>, Trp288 is part of the binding pocket. This position is homologues to Trp265 (6.48) of Rhodopsin which interacts with retinal (a tryptophan is in general conserved at this position in class A receptors and is thought to be involved in receptor signaling).

Revision as of 12:45, 8 October 2009 view source Anat Levit (talk \| contribs) 77 edits No edit summary ← Older edit		Revision as of 12:48, 8 October 2009 view source Anat Levit (talk \| contribs) 77 edits No edit summary Newer edit →
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	The ligand binding pocket of bovine Rhodopsin is similar in position to the β2-Adrenergic receptor binding site, and also involves TMs II, III, V and VI. The position does not vary considerably with alternate ligands or between different subtypes of different species. The retinal binding pocket relies mainly on hydrophobic interactions in addition to a covalent linkage with TM VII. In both, <scene name='User:Anat_Levit/Sandbox_1/Pkr1_1l9h_based_residues/3' target='PROKR1'>PROKR1</scene> and		The ligand binding pocket of bovine Rhodopsin is similar in position to the β2-Adrenergic receptor binding site, and also involves TMs II, III, V and VI. The position does not vary considerably with alternate ligands or between different subtypes of different species. The retinal binding pocket relies mainly on hydrophobic interactions in addition to a covalent linkage with TM VII. In both, <scene name='User:Anat_Levit/Sandbox_1/Pkr1_1l9h_based_residues/3' target='PROKR1'>PROKR1</scene> and
	<scene name='User:Anat_Levit/Sandbox_1/Pkr2_1l9h_residues/1' target='PROKR2'>PROKR2</scene>, Trp288 is part of the binding pocket. This position is homologues to Trp265 of Rhodopsin which interacts with retinal (a tryptophan is in general conserved at this position in class A receptors and is thought to be involved in receptor signaling).		<scene name='User:Anat_Levit/Sandbox_1/Pkr2_1l9h_residues/1' target='PROKR2'>PROKR2</scene>, Trp288 is part of the binding pocket. This position is homologues to Trp265 (6.48) of Rhodopsin which interacts with retinal (a tryptophan is in general conserved at this position in class A receptors and is thought to be involved in receptor signaling).