Ankyrin repeat domain-containing protein: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The 3D structure of the complex between human ARDCP 25 C-terminal and a kinesin peptide shows 2 types of interactions. Kinesin residues KARR interact in an acidic pocket and residues QMELLYA interact in a hydrophobic pocket<ref name="Guo"/>. | The 3D structure of the complex between human ARDCP 25 C-terminal and a kinesin peptide shows 2 types of interactions. Kinesin residues <scene name='86/863150/Cv/3'>KARR interact in an acidic pocket</scene> and residues <scene name='86/863150/Cv/4'>QMELLYA interact in a hydrophobic pocket</scene><ref name="Guo"/>. <scene name='86/863150/Cv/5'>Whole kinesin peptide binding site</scene>. | ||
</StructureSection> | </StructureSection> | ||