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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51310
VPS28 C-terminal domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51310

Description

The endosomal sorting complex I required for transport (ESCRT-I) is composed of the three subunits VPS23/TSG101, VPS28 and VPS37. ESCRT-I is recruited to cellular membranes during multivesicular endosome biogenesis and by enveloped viruses such as HIV-1 to mediate budding from the cell. The C-terminal domain of VPS28 is characterized by a high-sequence conservation throughout all kingdoms of life. It does not directly participate in ESCRT-I assembly (see <PDOC51312>) but serves as an adaptor module linked to the ESCRT-I complex that connects its function to other components of the VPS machinery, including ESCRT-III VPS20 [1].

The VPS28 C-terminal domain folds independently into a four-helical bundle structure with N- and C-terminal ends juxtaposed to each other (see <PDB:2G3K>). Helices 1, 2 and 4 have the same length, while helix 3 is shorter and packs with an approximate angle of 45 degrees against the remaining three helices. The connecting loop regions between helices 1 and 2 and helices 2 and 3 are short compared with the longer well-ordered loop connecting helices 3 and 4. Because this loop contains a conserved sequence motif, it may be involved in protein-protein interactions [1].

The profile we developed covers the entire VPS28 C-terminal domain.

Last update:

May 2007 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

VPS28_C, PS51310; VPS28 C-terminal domain profile  (MATRIX)


Reference

1AuthorsPineda-Molina E. Belrhali H. Piefer A.J. Akula I. Bates P. Weissenhorn W.
TitleThe crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment.
SourceTraffic 7:1007-1016(2006).
PubMed ID16749904
DOI10.1111/j.1600-0854.2006.00440.x



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