1zww
From Proteopedia
(New page: 200px<br /><applet load="1zww" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zww, resolution 2.30Å" /> '''Crystal structure of...) |
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| - | [[Image:1zww.gif|left|200px]]<br /><applet load="1zww" size=" | + | [[Image:1zww.gif|left|200px]]<br /><applet load="1zww" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zww, resolution 2.30Å" /> | caption="1zww, resolution 2.30Å" /> | ||
'''Crystal structure of endophilin-A1 BAR domain'''<br /> | '''Crystal structure of endophilin-A1 BAR domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Endophilin has been implicated in the retrieval of membrane via | + | Endophilin has been implicated in the retrieval of membrane via endocytosis of clathrin-coated vesicles, which is crucial for the maintenance of neurotransmitter exocytosis during stimulation; both exocytosis and endocytosis are regulated by intracellular calcium levels. Here, we present the 2.3 A crystal structure of the endophilin-A1 BAR domain, which has been suggested to function in inducing and sensing membrane curvature at the site of endocytosis. Endo-BAR folds into a crescent-shaped dimer composed of two elongated, three-helix bundles. Two additional domains of 30 residues each, inserted into helix 1 at the center of the concave side of the dimer, may interfere with the proposed mode of BAR domain membrane interaction. In addition, the dimer binds 11 divalent cadmium ions in the crystal mostly with typical Ca2+ co-ordination spheres. The endophilin-1A BAR domain thus constitutes a new variant of a BAR domain, and it may link endophilin-1A BAR function to calcium regulation of endocytosis. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZWW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZWW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: coiled coil]] | [[Category: coiled coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:52 2008'' |
Revision as of 14:19, 21 February 2008
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Crystal structure of endophilin-A1 BAR domain
Overview
Endophilin has been implicated in the retrieval of membrane via endocytosis of clathrin-coated vesicles, which is crucial for the maintenance of neurotransmitter exocytosis during stimulation; both exocytosis and endocytosis are regulated by intracellular calcium levels. Here, we present the 2.3 A crystal structure of the endophilin-A1 BAR domain, which has been suggested to function in inducing and sensing membrane curvature at the site of endocytosis. Endo-BAR folds into a crescent-shaped dimer composed of two elongated, three-helix bundles. Two additional domains of 30 residues each, inserted into helix 1 at the center of the concave side of the dimer, may interfere with the proposed mode of BAR domain membrane interaction. In addition, the dimer binds 11 divalent cadmium ions in the crystal mostly with typical Ca2+ co-ordination spheres. The endophilin-1A BAR domain thus constitutes a new variant of a BAR domain, and it may link endophilin-1A BAR function to calcium regulation of endocytosis.
About this Structure
1ZWW is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the endophilin-A1 BAR domain., Weissenhorn W, J Mol Biol. 2005 Aug 19;351(3):653-61. PMID:16023669
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