Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1074/jbc.M114.551176 http://scihub22266oqcxt.onion/10.1074/jbc.M114.551176 24706765!4031528!24706765     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2014 ; 289 (21): 14731-9 Nephropedia Template TP {{tp|p=24706765|t=2014. Mg2+-dependent interactions of ATP with the cystathionine-beta-synthase (CBS) domains of a magnesium transporter |pdf=|usr=}}{{24706765}} gab.com Text Mg2+-dependent interactions of ATP with the cystathionine-beta-synthase (CBS) domains of a magnesium transporter JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=24706765 #FOAvip Ancient conserved domain protein/cyclin M (CNNM) family proteins are evolutionarily conserved Mg(2+) transporters. However, their biochemical mechanism of action remains unknown. Here, we show the functional importance of the commonly conserved cystathionine-beta-synthase (CBS) domains and reveal their unique binding ability to ATP. Deletion mutants of CNNM2 and CNNM4, lacking the CBS domains, are unable to promote Mg(2+) efflux. Furthermore, the substitution of one amino acid residue in the CBS domains of CNNM2, which is associated with human hereditary hypomagnesemia, abrogates Mg(2+) efflux. Binding analyses reveal that the CBS domains of CNNM2 bind directly to ATP and not AMP in a manner dependent on the presence of Mg(2+), which is inhibited in a similar pattern by the disease-associated amino acid substitution. The requirement of Mg(2+) for these interactions is a unique feature among CBS domains, which can be explained by the presence of highly electronegative surface potentials around the ATP binding site on CNNM2. These results demonstrate that the CBS domains play essential roles in Mg(2+) efflux, probably through interactions with ATP. Interactions with ATP, which mostly forms complexes with Mg(2+) in cells, may account for the rapid Mg(2+) transport by CNNM family proteins. Twit Text FOAVip Mg2+-dependent interactions of ATP with the cystathionine-beta-synthase (CBS) domains of a magnesium transporter ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=24706765 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24706765 #FOAvip English Wikipedia <ref>{{Cite pmid|24706765}}</ref> Mg2+-dependent interactions of ATP with the cystathionine-beta-synthase (CBS) domains of a magnesium transporter #MMPMID24706765 Hirata Y; Funato Y; Takano Y; Miki H J Biol Chem 2014[May]; 289 (21): 14731-9 PMID24706765show ga Ancient conserved domain protein/cyclin M (CNNM) family proteins are evolutionarily conserved Mg(2+) transporters. However, their biochemical mechanism of action remains unknown. Here, we show the functional importance of the commonly conserved cystathionine-beta-synthase (CBS) domains and reveal their unique binding ability to ATP. Deletion mutants of CNNM2 and CNNM4, lacking the CBS domains, are unable to promote Mg(2+) efflux. Furthermore, the substitution of one amino acid residue in the CBS domains of CNNM2, which is associated with human hereditary hypomagnesemia, abrogates Mg(2+) efflux. Binding analyses reveal that the CBS domains of CNNM2 bind directly to ATP and not AMP in a manner dependent on the presence of Mg(2+), which is inhibited in a similar pattern by the disease-associated amino acid substitution. The requirement of Mg(2+) for these interactions is a unique feature among CBS domains, which can be explained by the presence of highly electronegative surface potentials around the ATP binding site on CNNM2. These results demonstrate that the CBS domains play essential roles in Mg(2+) efflux, probably through interactions with ATP. Interactions with ATP, which mostly forms complexes with Mg(2+) in cells, may account for the rapid Mg(2+) transport by CNNM family proteins. |Adenosine Triphosphate/*metabolism[MESH] |Amino Acid Sequence[MESH] |Amino Acid Substitution[MESH] |Animals[MESH] |Binding Sites/genetics[MESH] |Blotting, Western[MESH] |Cation Transport Proteins/chemistry/genetics/*metabolism[MESH] |Cystathionine beta-Synthase/*metabolism[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Ion Transport/genetics[MESH] |Magnesium/*metabolism[MESH] |Mice[MESH] |Microscopy, Confocal[MESH] |Models, Molecular[MESH] |Molecular Sequence Data[MESH] |Mutation[MESH] |Protein Binding/genetics[MESH] |Protein Structure, Tertiary[MESH] |Sequence Homology, Amino Acid[MESH]Mg2+-dependent interactions of ATP with the cystathionine-beta-synthas(epmc).pdf DeepDyve Pubget Overpricing