This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
SandboxCZ5
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ==Kinesin-1 Structure== | + | <scene name='80/809180/Kinesin_tubulin/1'>Text To Be Displayed</scene>==Kinesin-1 Structure== |
<StructureSection load='2y5w' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='2y5w' size='340' side='right' caption='Caption for this structure' scene=''> | ||
Kinesin-1, also known as a conventional kinesin, is a ATP-dependent molecular motor carrying its cargos towards the plus end of the microtubule. The structure shows its motor domains which perform the ATP-hydrolysis and actual movement along the microtubule. They are connected by a short part of its coiled-coil domain which continues to the autoinhibitory tail. | Kinesin-1, also known as a conventional kinesin, is a ATP-dependent molecular motor carrying its cargos towards the plus end of the microtubule. The structure shows its motor domains which perform the ATP-hydrolysis and actual movement along the microtubule. They are connected by a short part of its coiled-coil domain which continues to the autoinhibitory tail. | ||
== Function == | == Function == | ||
| - | + | <scene name='80/809180/Kinesin_tubulin/1'>The motot domain binds to microtubule.</scene> | |
== Disease == | == Disease == | ||
Current revision
==Kinesin-1 Structure==
| |||||||||||
