5mc7

Crystal structure of Truncated Human Coatomer Protein Complex, subunit Z1 (CopZ1)

spinqualitylabelsall models 5mc7, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mc7 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COPZ1_HUMAN The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex. Publication Abstract from PubMed The majority of modern anticancer approaches target DNA/protein targets involved in tumour-cell proliferation. Such approaches have a major drawback, as nonproliferating cancer cells remain unaffected and may cause relapse or remission. Human coatomer protein complex I (COPI) subunit zeta (Copzeta), a component of the coat protein involved in cell apoptosis and intracellular trafficking, has recently been proposed as a potential anticancer drug target. Previous studies have shown that two different isoforms of the Copzeta subunit exist in mammalian cells. While normal cells express both Copzeta1 and Copzeta2 isoforms, various types of tumour cells display a loss of Copzeta2 expression and rely solely on Copzeta1 for growth and survival. Subsequent knockdown of Copzeta1 results in specific inhibition of both proliferating and dormant tumour-cell populations, with no adverse growth effects on normal cells. Therefore, a Copzeta1-targeting therapy was proposed to bypass the problem of dormant cancer cells that are resistant to conventional antiproliferative drugs, which is the major cause of tumour relapse. In order to aid in structure-based inhibitor design, a crystal structure is required. In this article, the recombinant expression, purification, crystallization and crystal structure of Copzeta1, as well as the expression and purification of Copzeta2, are reported. Crystal structure of truncated human coatomer protein complex subunit zeta1 (Copzeta1).,Lunev S, Semmelink MF, Xian JL, Ma KY, Leenders AJ, Domling AS, Shtutman M, Groves MR Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):1-8. doi:, 10.1107/S2053230X16018896. Epub 2017 Jan 1. PMID:28045387 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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