1MFW

STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN

Summary for 1MFW

• Entry DOI: 10.2210/pdb1mfw/pdb
• Related: 1MG4 1MJD
• Descriptor: DOUBLECORTIN-LIKE KINASE (N-TERMINAL DOMAIN), SULFATE ION (3 entities in total)
• Functional Keywords: doublecortin, doublecortin-like kinase, microtubule bundling, cortex development, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 12443.92

Authors

Kim, M.H.,Cierpickil, T.,Derewenda, U.,Krowarsch, D.,Feng, Y.,Devedjiev, Y.,Dauter, Z.,Walsh, C.A.,Otlewski, J.,Bushweller, J.H.,Derewenda, Z. (deposition date: 2002-08-13, release date: 2003-04-29, Last modification date: 2024-10-30)

Primary citation

Kim, M.H.,Cierpickil, T.,Derewenda, U.,Krowarsch, D.,Feng, Y.,Devedjiev, Y.,Dauter, Z.,Walsh, C.A.,Otlewski, J.,Bushweller, J.H.,Derewenda, Z.
The DCX-domain Tandems of Doublecortin and Doublecortin-like Kinase
Nat.Struct.Biol., 10:324-333, 2003

PubMed Abstract: The doublecortin-like domains (DCX), which typically occur in tandem, are novel microtubule-binding modules. DCX tandems are found in doublecortin, a 360-residue protein expressed in migrating neurons; the doublecortin-like kinase (DCLK); the product of the RP1 gene that is responsible for a form of inherited blindness; and several other proteins. Mutations in the gene encoding doublecortin cause lissencephaly in males and the 'double-cortex syndrome' in females. We here report a solution structure of the N-terminal DCX domain of human doublecortin and a 1.5 A resolution crystal structure of the equivalent domain from human DCLK. Both show a stable, ubiquitin-like tertiary fold with distinct structural similarities to GTPase-binding domains. We also show that the C-terminal DCX domains of both proteins are only partially folded. In functional assays, the N-terminal DCX domain of doublecortin binds only to assembled microtubules, whereas the C-terminal domain binds to both microtubules and unpolymerized tubulin.

PubMed: 12692530
DOI: 10.1038/nsb918

Experimental method

X-RAY DIFFRACTION (1.6 Å)