Feedback of the kinesin-1 neck-linker position on the catalytic site
| Autor: | Guenther Woehlke, Katrin Hahlen, Judith Mergler, Albert Sickmann, Jörg Reinders, Bettina Ebbing |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Binding Sites Neurospora crassa Chemistry Protein Conformation Kinesins Cell Biology Biochemistry Microtubules Motor domain Motor protein Adenosine Diphosphate Fungal Proteins Crystallography Structure-Activity Relationship Adenosine Triphosphate Microtubule Catalytic Domain Biophysics Kinesin Tyrosine Binding site Molecular Biology Linker Protein Binding |
| Zdroj: | The Journal of biological chemistry. 281(27) |
| ISSN: | 0021-9258 |
| Popis: | Kinesin-1 motor proteins step along microtubules by a mechanism in which the heads cycle through microtubule-bound and unbound states in an interlaced fashion. An important contribution to head-head coordination arises from the action of the neck-linker that docks onto the core motor domain upon ATP binding. We show here that the docked neck-linker not only guides the microtubule-unbound head to the next microtubule binding site but also signals its position to the head to which it is attached. Cross-linking studies on mutated kinesin constructs reveal that residues at the interface motor core/docked neck-linker, among them most importantly a conserved tyrosine, are involved in this feedback. The primary effect of the docked neck-linker is a reduced microtubule binding affinity in the ADP state. |
| Databáze: | OpenAIRE |
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