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10.3390/ijms20246279 http://scihub22266oqcxt.onion/10.3390/ijms20246279 31842432!6940986!31842432     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Mol+Sci 2019 ; 20 (24): ä Nephropedia Template TP {{tp|p=31842432|t=2019. Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4 |pdf=|usr=}}{{31842432}} gab.com Text Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4 JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=31842432 #FOAvip The four member family of "Cyclin and Cystathionine beta-synthase (CBS) domain divalent metal cation transport mediators", CNNMs, are the least-studied mammalian magnesium transport mediators. CNNM4 is abundant in the brain and the intestinal tract, and its abnormal activity causes Jalili Syndrome. Recent findings show that suppression of CNNM4 in mice promotes malignant progression of intestinal polyps and is linked to infertility. The association of CNNM4 with phosphatases of the regenerating liver, PRLs, abrogates its Mg(2+)-efflux capacity, thus resulting in an increased intracellular Mg(2+) concentration that favors tumor growth. Here we present the crystal structures of the two independent intracellular domains of human CNNM4, i.e., the Bateman module and the cyclic nucleotide binding-like domain (cNMP). We also derive a model structure for the full intracellular region in the absence and presence of MgATP and the oncogenic interacting partner, PRL-1. We find that only the Bateman module interacts with ATP and Mg(2+), at non-overlapping sites facilitating their positive cooperativity. Furthermore, both domains dimerize autonomously, where the cNMP domain dimer forms a rigid cleft to restrict the Mg(2+) induced sliding of the inserting CBS1 motives of the Bateman module, from a twisted to a flat disk shaped dimer. Twit Text FOAVip Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4 ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=31842432 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=31842432 #FOAvip English Wikipedia <ref>{{Cite pmid|31842432}}</ref> Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4 #MMPMID31842432 Gimenez-Mascarell P; Oyenarte I; Gonzalez-Recio I; Fernandez-Rodriguez C; Corral-Rodriguez MA; Campos-Zarraga I; Simon J; Kostantin E; Hardy S; Diaz Quintana A; Zubillaga Lizeaga M; Merino N; Diercks T; Blanco FJ; Diaz Moreno I; Martinez-Chantar ML; Tremblay ML; Muller D; Siliqi D; Martinez-Cruz LA Int J Mol Sci 2019[Dec]; 20 (24): ä PMID31842432show ga The four member family of "Cyclin and Cystathionine beta-synthase (CBS) domain divalent metal cation transport mediators", CNNMs, are the least-studied mammalian magnesium transport mediators. CNNM4 is abundant in the brain and the intestinal tract, and its abnormal activity causes Jalili Syndrome. Recent findings show that suppression of CNNM4 in mice promotes malignant progression of intestinal polyps and is linked to infertility. The association of CNNM4 with phosphatases of the regenerating liver, PRLs, abrogates its Mg(2+)-efflux capacity, thus resulting in an increased intracellular Mg(2+) concentration that favors tumor growth. Here we present the crystal structures of the two independent intracellular domains of human CNNM4, i.e., the Bateman module and the cyclic nucleotide binding-like domain (cNMP). We also derive a model structure for the full intracellular region in the absence and presence of MgATP and the oncogenic interacting partner, PRL-1. We find that only the Bateman module interacts with ATP and Mg(2+), at non-overlapping sites facilitating their positive cooperativity. Furthermore, both domains dimerize autonomously, where the cNMP domain dimer forms a rigid cleft to restrict the Mg(2+) induced sliding of the inserting CBS1 motives of the Bateman module, from a twisted to a flat disk shaped dimer. |Adenosine Triphosphate/chemistry/metabolism[MESH] |Amino Acid Sequence[MESH] |Binding Sites[MESH] |Biological Transport[MESH] |Cation Transport Proteins/*chemistry/*metabolism[MESH] |Humans[MESH] |Magnesium/chemistry/*metabolism[MESH] |Magnetic Resonance Spectroscopy[MESH] |Models, Molecular[MESH] |Molecular Conformation[MESH] |Protein Binding[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Multimerization[MESH]Structural Insights into the Intracellular Region of the Human Magnesi(epmc).pdf DeepDyve Pubget Overpricing