Detail An ATP Gate Controls Tubulin Binding by the Tethered Head of Kinesin-1   Oleh:  Alonso, Maria C. ; Drumond, Douglass R ; Kain, Susan ; Hoeng, Julia ; Amos, Linda ; Cross, Robert A Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 316 no. 5821 (Apr. 2007), page 120. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.04 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel Kinesin-l is a two-headed molecular motor that walks along microtubules, with each step gated by adenosine triphosphate (ATP) binding. Existing models for the gating mechanism propose a role for the microtubule lattice. We show that unpolymerized tubulin binds to kinesin-l, causing tubulin-activated release of adenosine diphosphate (ADP). With no added nucleotide, each kinesin-l dimer binds one tubulin heterodimer. In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable ATP analog, each kinesin-l dimer binds two tubulin heterodimers. The data reveal an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of a steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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