1wr0

File:1wr0.gif

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Structural characterization of the MIT domain from human Vps4b

OverviewOverview

The microtubule interacting and trafficking (MIT) domain is a small, protein module of unknown function that is conserved in proteins of, diverse function, such as Vps4, sorting nexin 15 (SNX15), and spastin. One, non-synonymous single nucleotide polymorphism was reported, which results, in a Ile58-to-Met (I58M) substitution in hVps4b. Here, we have determined, the solution structure of the MIT domain isolated from the NH(2)-terminus, of human Vps4b, an AAA-ATPase involved in multivesicular body formation., The MIT domain adopts an 'up-and-down' three-helix bundle. Comparison with, the sequences of other MIT domains clearly shows that the residues, involved in inter-helical contacts are well conserved. The Ile58-to-Met, substitution resulted a substantial thermal instability. In addition, we, found a shallow crevice between helices A and C that may serve as a, protein-binding site. We propose that the MIT domain serves as a putative, adaptor domain for the ESCRT-III complex involved in endosomal, trafficking.

About this StructureAbout this Structure

1WR0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural characterization of the MIT domain from human Vps4b., Takasu H, Jee JG, Ohno A, Goda N, Fujiwara K, Tochio H, Shirakawa M, Hiroaki H, Biochem Biophys Res Commun. 2005 Aug 26;334(2):460-5. PMID:16018968

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