ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Purification, crystallization and preliminary crystallographic analysis of the CBS pair of the human metal transporter CNNM4.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- A novel mutation in CNNM4 is associated with a case of Jalili syndrome in Egypt.Documenta ophthalmologica. Advances in ophthalmology · 2025Article
- Expanding the genotypic spectrum of Jalili syndrome: Novel CNNM4 variants and uniparental isodisomy in a north American patient cohort.American journal of medical genetics. Part A · 2020Article
- Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4.International journal of molecular sciences · 2019Article
- A novel pathogenic missense variant in CNNM4 underlying Jalili syndrome: Insights from molecular dynamics simulations.Molecular genetics & genomic medicine · 2019Article
- Nucleotide binding triggers a conformational change of the CBS module of the magnesium transporter CNNM2 from a twisted towards a flat structure.The Biochemical journal · 2014Article
- Improving the chances of successful protein structure determination with a random forest classifier.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Purification, crystallization and preliminary crystallographic analysis of the CBS-domain pair of cyclin M2 (CNNM2).Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Membrane topology and intracellular processing of cyclin M2 (CNNM2).The Journal of biological chemistry · 2012Article
- Crystals on the cover 2012.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This work describes the purification and preliminary crystallographic analysis of the CBS-pair regulatory domain of the human ancient domain protein 4 (ACDP4), also known as CNNM4. ACDP proteins represent the least-studied members of the eight different types of magnesium transporters that have been identified in mammals to date. In humans the ACDP family includes four members: CNNM1-4. CNNM1 acts as a cytosolic copper chaperone and has been associated with urofacial syndrome, whereas CNNM2 and CNNM4 have been identified as magnesium transporters. Interestingly, mutations in the CNNM4 gene have clinical consequences that are limited to retinal function and biomineralization and are considered to be the cause of Jalili syndrome, which consists of autosomal recessive cone-rod dystrophy and amelogenesis imperfecta. The truncated protein was overexpressed, purified and crystallized in the orthorhombic space group C222. The crystals diffracted X-rays to 3.6 Å resolution using synchrotron radiation. Matthews volume calculations suggested the presence of two molecules in the asymmetric unit, which were likely to correspond to a CBS module of the CBS pair of CNNM4.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.