Charged multivesicular body protein

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== Structural highlights ==
== Structural highlights ==
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The ampiphatic CHMP5 creates a hydrophobic binding collar that includes <scene name='80/803956/Cv/3'>6 invariant Leu residues</scene> which make <scene name='80/803956/Cv/4'>hydrophobic interactions with the vacuolar protein sorting-associated protein Vta1 homolog</scene>. A strong charge complementarity is formed between CHMP5 negative surface which includes 13 Asp and Glu residues and 11 basic residues on the vacuolar protein sorting-associated protein Vta1 homolog binding surface<ref>PMID:23105106</ref>.
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The ampiphatic CHMP5 creates a hydrophobic binding collar that includes <scene name='80/803956/Cv/3'>6 invariant Leu residues</scene> which make <scene name='80/803956/Cv/4'>hydrophobic interactions with the vacuolar protein sorting-associated protein Vta1 homolog</scene>. A <scene name='80/803956/Cv/5'>strong charge complementarity</scene> is formed between CHMP5 negative surface which includes 13 Asp and Glu residues and 11 basic residues on the vacuolar protein sorting-associated protein Vta1 homolog binding surface<ref>PMID:23105106</ref>.
</StructureSection>
</StructureSection>

Revision as of 12:00, 18 December 2018

Human CHMP5 residues 139-195 (green) complex with vacuolar protein sorting-associated protein Vta1 homolog (cyan) (PDB code 2lxm)

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3D structures of charged multivesicular body protein

Updated on 18-December-2018

References

  1. ↑ Schmidt O, Teis D. The ESCRT machinery. Curr Biol. 2012 Feb 21;22(4):R116-20. doi: 10.1016/j.cub.2012.01.028. PMID:22361144 doi:http://dx.doi.org/10.1016/j.cub.2012.01.028
  2. ↑ Spitzer C, Li F, Buono R, Roschzttardtz H, Chung T, Zhang M, Osteryoung KW, Vierstra RD, Otegui MS. The endosomal protein CHARGED MULTIVESICULAR BODY PROTEIN1 regulates the autophagic turnover of plastids in Arabidopsis. Plant Cell. 2015 Feb;27(2):391-402. doi: 10.1105/tpc.114.135939. Epub 2015 Feb 3. PMID:25649438 doi:http://dx.doi.org/10.1105/tpc.114.135939
  3. ↑ Bodon G, Chassefeyre R, Pernet-Gallay K, Martinelli N, Effantin G, Hulsik DL, Belly A, Goldberg Y, Chatellard-Causse C, Blot B, Schoehn G, Weissenhorn W, Sadoul R. Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane. J Biol Chem. 2011 Nov 18;286(46):40276-86. doi: 10.1074/jbc.M111.283671. Epub, 2011 Sep 16. PMID:21926173 doi:http://dx.doi.org/10.1074/jbc.M111.283671
  4. ↑ Parkinson N, Ince PG, Smith MO, Highley R, Skibinski G, Andersen PM, Morrison KE, Pall HS, Hardiman O, Collinge J, Shaw PJ, Fisher EM. ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B). Neurology. 2006 Sep 26;67(6):1074-7. Epub 2006 Jun 28. PMID:16807408 doi:10.1212/01.wnl.0000231510.89311.8b
  5. ↑ Skalicky JJ, Arii J, Wenzel DM, Stubblefield WM, Katsuyama A, Uter NT, Bajorek M, Myszka DG, Sundquist WI. Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport. J Biol Chem. 2012 Oct 26. PMID:23105106 doi:http://dx.doi.org/10.1074/jbc.M112.417899

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