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.
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Nucleotide Pocket Configuration
Contrast With MT-Bound Conformations
Functional Relevance of L11
L11, flexible and undocked in the ADP state, emerges as a central determinant of microtubule nucleotide-state sensing. Mutations in L11 abolish KIF5C’s preference for GTP-state microtubules and reduce MT-activated ATPase activity.
Conclusion
The 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.
