Charged multivesicular body protein: Difference between revisions
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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>. | 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>. | ||
==3D structures of charged multivesicular body protein== | |||
[[Charged multivesicular body protein 3D structures]] | |||
</StructureSection> | </StructureSection> | ||