M-type motors

In spite of the gross conformational differences between the Ned dimers, there are only minor differences between the individual motor domains. The overall fold of the motor domain is very similar to that of kinesin-1 and other N-type motors. Major differences are (1) The N-terminal lobe of Ned is enlarged (+9 amino acids) compared with rat kinesin-1. The additional residues are located between /11b and /11c (the L2 finger ). This, however, does not result in a simple elongation of the /1-hairpin as in HsKSP and in M-type motors (see below). In fact, the tip of the L2 finger is rather broadened and forms a short a-helix. (2) Loop L5, the insert in the P-loop helix z 2. is quite short (approximately eight residues compared with 12 in rat kinesin-1), due to three residues that are missing in the primary structure of DmNcd. (3) Switch-1 helix z.3 is short and loop L9, the linker between z.3 and / 6 that includes the switch-1... 

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