Abstract
Coordination between Motor Domains in Processive Kinesins
Highlights
These models differ, for conventional kinesin dimer the favored one predicts that the two kinesin heads bind alternatively to the track, taking 80-Å steps along the microtubule while hydrolyzing one ATP molecule per step (4 – 6)
We review the phenomenon of kinesin processivity from a complementary perspective by considering specific structural features of the motor domains that underlie their coordination
All kinesins share the conserved catalytic core (residues Asn8–Ala322 in human kinesin [19]), which consists of a central -sheet sandwiched between six ␣-helices (Fig. 1A, cream) and a topologically conserved smaller lobe (Fig. 1A, peach) with three additional -strands
Summary
Among cellular functions that kinesins perform, their ability to walk along the microtubules transporting specific cargoes is the most fascinating [1, 2] The complexity of this phenomenon and tremendous scientific efforts put toward dissecting the mechanisms underlying it have led to conflicting models explaining how kinesins might travel long distances without dissociating from their biological track (e.g. move “processively” [3]). These models differ, for conventional kinesin dimer the favored one predicts that the two kinesin heads bind alternatively to the track, taking 80-Å steps along the microtubule while hydrolyzing one ATP molecule per step (4 – 6). We review the phenomenon of kinesin processivity from a complementary perspective by considering specific structural features of the motor domains that underlie their coordination
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