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Article

Structural and mechanistic studies of VPS4 proteins.

The EMBO journal - 19 Oct 2005

Scott Anna, Chung Hyo-Young, Gonciarz-Swiatek Malgorzata, Hill Gina C, Whitby Frank G, Gaspar Jason, Holton James M, Viswanathan Ramya, Ghaffarian Sanaz, Hill Christopher P, Sundquist Wesley I

Abstract excerpt

VPS4 ATPases function in multivesicular body formation and in HIV-1 budding. Here, we report the crystal structure of monomeric apo human VPS4B/SKD1 (hVPS4B), which is composed of five distinct elements: a poorly ordered N-terminal MIT domain that binds ESCRT-III substrates, large (mixed alpha/beta) and small (alpha) AAA ATPase domains that closely resemble analogous domains in the p97 D1 ATPase cassette, a...

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Share to Adenosine Triphosphatases
Share to ATPases Associated with Diverse Cellular Activities

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Endosomal Sorting Complexes Required for Transport

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Identifiers

PMID: 16193069
DOI: 10.1038/sj.emboj.7600818
PMCID: PMC1276703

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Structural and mechanistic studies of VPS4 proteins.PMID 16193069Read ↗

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