Crystal Structure of the KIF5C Motor Domain With ADP
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This is a default text for your page Crystal Structure of the KIF5C Motor Domain With ADP. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. ContentsNucleotide Pocket ConfigurationContrast With MT-Bound ConformationsFunctional Relevance of L11ConclusionThe ADP structure provides a mechanistic baseline, clarifying how GTP-state microtubule recognition reshapes the KIF5C motor into its force-generating form. Because GTP-state lattices are enriched in axons relative to dendrites, this structural preference directly explains why KIF5C selectively enters axons and not dendrites. Accordingly, the ADP-bound conformation represents a primed intermediate that supports polarised neuronal transport upon recognition of the appropriate microtubule substrate.
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