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.
Kinesin
From Proteopedia
3D Structure of Kinesin
The image is a Crystal Structure of the Kif1A Motor Domain Before Mg Release (2zfi)
Kinesin
Kinesins are eukaryotic motor proteins which move along microtubules. Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains. The heavy chain contains the globular motor domain (MD), flexible neck linker (FNL) and a long coiled-coil stalk which intertwines to form the dimer. The light chain (KLC) forms the tail region. The KLC contains a cargo binding domain which is called TPR (Tetratricopeptide repeat). The KIFs are named by their gene number. KIF contains a forkhead-associated domain (FHA) which is involved in phosphopeptide recognition. Kinesin protein in yeast is called Kar3. Eg5 or KIF11 is a kinesin (Kinesin-5) which participates in mitosis. KCBP is a Kinesin-like Calmodulin Binding Protein. NOD is a Drosophila chromosome-associated kinesin. See also CAP-Gly domain.
3D Structures of Kinesin
Updated on 31-January-2016
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, David Canner, Joel L. Sussman, Jaime Prilusky
