3ZXP

Structural and Functional Analyses of the Bro1 Domain Protein BROX

Summary for 3ZXP

• Entry DOI: 10.2210/pdb3zxp/pdb
• Descriptor: BRO1 DOMAIN-CONTAINING PROTEIN BROX (2 entities in total)
• Functional Keywords: protein transport
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Membrane; Lipid-anchor (Potential): Q5VW32
• Total number of polymer chains: 3
• Total formula weight: 138223.32

Authors

Zhai, Q.,Landesman, M.B.,Sundquist, W.I.,Hill, C.P. (deposition date: 2011-08-13, release date: 2011-11-16, Last modification date: 2024-05-08)

Primary citation

Zhai, Q.,Landesman, M.B.,Robinson, H.,Sundquist, W.I.,Hill, C.P.
Structure of the Bro1 Domain Protein Brox and Functional Analyses of the Alix Bro1 Domain in HIV-1 Budding.
Plos One, 6:27466-, 2011

PubMed Abstract: Bro1 domains are elongated, banana-shaped domains that were first identified in the yeast ESCRT pathway protein, Bro1p. Humans express three Bro1 domain-containing proteins: ALIX, BROX, and HD-PTP, which function in association with the ESCRT pathway to help mediate intraluminal vesicle formation at multivesicular bodies, the abscission stage of cytokinesis, and/or enveloped virus budding. Human Bro1 domains share the ability to bind the CHMP4 subset of ESCRT-III proteins, associate with the HIV-1 NC(Gag) protein, and stimulate the budding of viral Gag proteins. The curved Bro1 domain structure has also been proposed to mediate membrane bending. To date, crystal structures have only been available for the related Bro1 domains from the Bro1p and ALIX proteins, and structures of additional family members should therefore aid in the identification of key structural and functional elements.

PubMed: 22162750
DOI: 10.1371/JOURNAL.PONE.0027466

Experimental method

X-RAY DIFFRACTION (2.495 Å)