4frz

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Template:STRUCTURE 4frz

Contents

Arabidopsis KCBP motor domain dimerized via regulatory domain

Template:ABSTRACT PUBMED 23805258

Function

[KCBP_ARATH] Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis. Possesses basal and microtubule-stimulated ATPase activities.[1] [2] [3] [4] [5]

About this Structure

4frz is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

  • Vinogradova MV, Malanina GG, Waitzman JS, Rice SE, Fletterick RJ. Plant Kinesin-Like Calmodulin Binding Protein Employs Its Regulatory Domain for Dimerization. PLoS One. 2013 Jun 21;8(6):e66669. Print 2013. PMID:23805258 doi:10.1371/journal.pone.0066669
  1. ↑ Reddy AS, Safadi F, Narasimhulu SB, Golovkin M, Hu X. A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain. J Biol Chem. 1996 Mar 22;271(12):7052-60. PMID:8636137
  2. ↑ Oppenheimer DG, Pollock MA, Vacik J, Szymanski DB, Ericson B, Feldmann K, Marks MD. Essential role of a kinesin-like protein in Arabidopsis trichome morphogenesis. Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6261-6. PMID:9177205
  3. ↑ Deavours BE, Reddy AS, Walker RA. Ca2+/calmodulin regulation of the Arabidopsis kinesin-like calmodulin-binding protein. Cell Motil Cytoskeleton. 1998;40(4):408-16. PMID:9712269 doi:<408::AID-CM8>3.0.CO;2-6 10.1002/(SICI)1097-0169(1998)40:4<408::AID-CM8>3.0.CO;2-6
  4. ↑ Narasimhulu SB, Reddy AS. Characterization of microtubule binding domains in the Arabidopsis kinesin-like calmodulin binding protein. Plant Cell. 1998 Jun;10(6):957-65. PMID:9634584
  5. ↑ Reddy VS, Day IS, Thomas T, Reddy AS. KIC, a novel Ca2+ binding protein with one EF-hand motif, interacts with a microtubule motor protein and regulates trichome morphogenesis. Plant Cell. 2004 Jan;16(1):185-200. Epub 2003 Dec 19. PMID:14688294 doi:10.1105/tpc.016600

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