2csa
From Proteopedia
(New page: 200px<br /> <applet load="2csa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2csa" /> '''Structure of the M3 Muscarinic Acetylcholin...) |
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'''Structure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal'''<br /> | '''Structure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Muscarinic acetylcholine receptors comprise a family of G-protein-coupled | + | Muscarinic acetylcholine receptors comprise a family of G-protein-coupled receptors that display differential localization in polarized epithelial cells. We identify a seven-residue sequence, Ala(275)-Val(281), in the third intracellular loop of the M(3) muscarinic receptor that mediates dominant, position-independent basolateral targeting in Madin-Darby canine kidney cells. Mutational analyses identify Glu(276), Phe(280), and Val(281) as critical residues within this sorting motif. Phe(280) and Val(281) comprise a novel dihydrophobic sorting signal as mutations of either residue singly or together with leucine do not disrupt basolateral targeting. Conversely, Glu(276) is required and cannot be substituted with alanine or aspartic acid. A 19-amino acid peptide representing the M(3) sorting signal and surrounding sequence was analyzed via two-dimensional nuclear magnetic resonance spectroscopy. Solution structures show that Glu(276) resides in a type IV beta-turn and the dihydrophobic sequence Phe(280)Val(281) adopts either a type I or IV beta-turn. |
==About this Structure== | ==About this Structure== | ||
| - | 2CSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 2CSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CSA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fox, D.]] | [[Category: Fox, D.]] | ||
| - | [[Category: Iverson, H | + | [[Category: Iverson, H A.]] |
| - | [[Category: Klevit, R | + | [[Category: Klevit, R E.]] |
| - | [[Category: Nadler, L | + | [[Category: Nadler, L S.]] |
| - | [[Category: Nathanson, N | + | [[Category: Nathanson, N M.]] |
[[Category: basolateral sorting-signal blss beta-turn]] | [[Category: basolateral sorting-signal blss beta-turn]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:02 2008'' |
Revision as of 14:52, 21 February 2008
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Structure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal
Overview
Muscarinic acetylcholine receptors comprise a family of G-protein-coupled receptors that display differential localization in polarized epithelial cells. We identify a seven-residue sequence, Ala(275)-Val(281), in the third intracellular loop of the M(3) muscarinic receptor that mediates dominant, position-independent basolateral targeting in Madin-Darby canine kidney cells. Mutational analyses identify Glu(276), Phe(280), and Val(281) as critical residues within this sorting motif. Phe(280) and Val(281) comprise a novel dihydrophobic sorting signal as mutations of either residue singly or together with leucine do not disrupt basolateral targeting. Conversely, Glu(276) is required and cannot be substituted with alanine or aspartic acid. A 19-amino acid peptide representing the M(3) sorting signal and surrounding sequence was analyzed via two-dimensional nuclear magnetic resonance spectroscopy. Solution structures show that Glu(276) resides in a type IV beta-turn and the dihydrophobic sequence Phe(280)Val(281) adopts either a type I or IV beta-turn.
About this Structure
2CSA is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Identification and structural determination of the M(3) muscarinic acetylcholine receptor basolateral sorting signal., Iverson HA, Fox D 3rd, Nadler LS, Klevit RE, Nathanson NM, J Biol Chem. 2005 Jul 1;280(26):24568-75. Epub 2005 May 2. PMID:15870063
Page seeded by OCA on Thu Feb 21 16:52:02 2008
