Journal Article

PUBDB-2017-09765

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The Coiled-Coil Helix in the Neck of Kinesin

Thormählen, M. ; Marx, A.CFEL*MPG* ; Sack, S. ; Mandelkow, E.MPG*

1998
Elsevier San Diego, Calif.

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Please use a persistent id in citations: doi:10.1006/jsbi.1998.3986

Abstract: Kinesin is a microtubule-dependent motor protein. We have recently determined the X-ray structure of monomeric and dimeric kinesin from rat brain. The dimer consists of two motor domains, held together by their α-helical neck domains forming a coiled coil. Here we analyze the nature of the interactions in the neck domain (residues 339–370). Overall, the neck helix shows a heptad repeat (abcdefg)ntypical of coiled coils, with mostly nonpolar residues in positions a and d. However, the first segment (339–355) contains several nonclassical residues in the a and d positions which tend to weaken the hydrophobic interaction along the common interface. Instead, stabilization is achieved by a hydrophobic “coat” formed by the a and d residues and the long aliphatic moieties of lysines and glutamates, extending away from the coiled-coil core. By contrast, the second segment of the kinesin neck (356–370) shows a classical leucine zipper pattern in which most of the hydrophobic residues are buried at the highly symmetrical dimer interface. The end of the neck reveals the structure of a potential coiled-coil “trigger” sequence.

Note: F-Bereich; Max-Planck-Gesellschaft

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Contributing Institute(s):

1. DESY Retrocat (DESY(-2012))

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Experiment(s):

1. No specific instrument

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Database coverage:
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