2raj

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(New page: 200px<br /><applet load="2raj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2raj, resolution 2.45&Aring;" /> '''SO4 bound PX-BAR mem...)
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==Overview==
==Overview==
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Sorting nexins (SNXs) form a family of proteins known to interact with, components in the endosomal system and to regulate various steps of, vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages, of clathrin-mediated endocytosis in non-neuronal cells, where together, with the GTPase dynamin, it participates in the formation and scission of, the vesicle neck. We report here crystal structures of the functional, membrane-remodeling unit of SNX9 and show that it efficiently tubulates, lipid membranes in vivo and in vitro. Elucidation of the protein, superdomain structure, together with mutational analysis and biochemical, and cell biological experiments, demonstrated how the SNX9 PX and BAR, domains work in concert in targeting and tubulation of, phosphoinositide-containing membranes. The study provides insights into, the SNX9-induced membrane modulation mechanism.
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Sorting nexins (SNXs) form a family of proteins known to interact with components in the endosomal system and to regulate various steps of vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages of clathrin-mediated endocytosis in non-neuronal cells, where together with the GTPase dynamin, it participates in the formation and scission of the vesicle neck. We report here crystal structures of the functional membrane-remodeling unit of SNX9 and show that it efficiently tubulates lipid membranes in vivo and in vitro. Elucidation of the protein superdomain structure, together with mutational analysis and biochemical and cell biological experiments, demonstrated how the SNX9 PX and BAR domains work in concert in targeting and tubulation of phosphoinositide-containing membranes. The study provides insights into the SNX9-induced membrane modulation mechanism.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Carlsson, S.R.]]
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[[Category: Carlsson, S R.]]
[[Category: Lundmark, R.]]
[[Category: Lundmark, R.]]
[[Category: Pylypenko, O.]]
[[Category: Pylypenko, O.]]
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[[Category: tubulation]]
[[Category: tubulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:45:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:45:56 2008''

Revision as of 16:45, 21 February 2008


2raj, resolution 2.45Å

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SO4 bound PX-BAR membrane remodeling unit of Sorting Nexin 9

Overview

Sorting nexins (SNXs) form a family of proteins known to interact with components in the endosomal system and to regulate various steps of vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages of clathrin-mediated endocytosis in non-neuronal cells, where together with the GTPase dynamin, it participates in the formation and scission of the vesicle neck. We report here crystal structures of the functional membrane-remodeling unit of SNX9 and show that it efficiently tubulates lipid membranes in vivo and in vitro. Elucidation of the protein superdomain structure, together with mutational analysis and biochemical and cell biological experiments, demonstrated how the SNX9 PX and BAR domains work in concert in targeting and tubulation of phosphoinositide-containing membranes. The study provides insights into the SNX9-induced membrane modulation mechanism.

About this Structure

2RAJ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The PX-BAR membrane-remodeling unit of sorting nexin 9., Pylypenko O, Lundmark R, Rasmuson E, Carlsson SR, Rak A, EMBO J. 2007 Nov 14;26(22):4788-800. Epub 2007 Oct 18. PMID:17948057

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