2r17
From Proteopedia
(New page: 200px<br /> <applet load="2r17" size="450" color="white" frame="true" align="right" spinBox="true" caption="2r17, resolution 2.80Å" /> '''Functional architec...) |
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caption="2r17, resolution 2.80Å" /> | caption="2r17, resolution 2.80Å" /> | ||
'''Functional architecture of the retromer cargo-recognition complex'''<br /> | '''Functional architecture of the retromer cargo-recognition complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2R17 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2R17 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R17 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein transport]] | [[Category: protein transport]] | ||
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Revision as of 10:38, 23 January 2008
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Functional architecture of the retromer cargo-recognition complex
Overview
The retromer complex is required for the sorting of acid hydrolases to, lysosomes, transcytosis of the polymeric immunoglobulin receptor, Wnt, gradient formation, iron transporter recycling and processing of the, amyloid precursor protein. Human retromer consists of two smaller, complexes: the cargo recognition VPS26-VPS29-VPS35 heterotrimer and a, membrane-targeting heterodimer or homodimer of SNX1 and/or SNX2 (ref. 13)., Here we report the crystal structure of a VPS29-VPS35 subcomplex showing, how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a, scaffold for the carboxy-terminal half of VPS35. VPS35 forms a, horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face, of which completely covers the metal-binding site of VPS29, whereas the, convex face exposes a series of hydrophobic interhelical grooves. Electron, microscopy shows that the intact VPS26-VPS29-VPS35 complex is a, stick-shaped, flexible structure, approximately 21 nm long. A hybrid, structural model derived from crystal structures, electron microscopy, interaction studies and bioinformatics shows that the alpha-solenoid fold, extends the full length of VPS35, and that VPS26 is bound at the opposite, end from VPS29. This extended structure presents multiple binding sites, for the SNX complex and receptor cargo, and appears capable of flexing to, conform to curved vesicular membranes.
About this Structure
2R17 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Functional architecture of the retromer cargo-recognition complex., Hierro A, Rojas AL, Rojas R, Murthy N, Effantin G, Kajava AV, Steven AC, Bonifacino JS, Hurley JH, Nature. 2007 Oct 25;449(7165):1063-7. Epub 2007 Sep 23. PMID:17891154
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