Sökning: onr:"swepub:oai:DiVA.org:su-25485" > Crystal structure o...
Fältnamn | Indikatorer | Metadata |
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000 | 02689naa a2200409 4500 | |
001 | oai:DiVA.org:su-25485 | |
003 | SwePub | |
008 | 080922s2007 | |||||||||||000 ||eng| | |
009 | oai:prod.swepub.kib.ki.se:115585103 | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-254852 URI |
024 | 7 | a https://doi.org/10.1074/jbc.M6048522002 DOI |
024 | 7 | a http://kipublications.ki.se/Default.aspx?queryparsed=id:1155851032 URI |
040 | a (SwePub)sud (SwePub)ki | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Bakali, Aminu Stockholms universitet,Institutionen för biokemi och biofysik4 aut |
245 | 1 0 | a Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site |
264 | 1 | c 2007 |
338 | a print2 rdacarrier | |
520 | a The human lipid kinase family controls cell proliferation, differentiation, and tumorigenesis and includes diacylglycerol kinases, sphingosine kinases, and ceramide kinases. YegS is an Escherichia coli protein with significant sequence homology to the catalytic domain of the human lipid kinases. We have solved the crystal structure of YegS and shown that it is a lipid kinase with phosphatidylglycerol kinase activity. The crystal structure reveals a two-domain protein with significant structural similarity to a family of NAD kinases. The active site is located in the interdomain cleft formed by four conserved sequence motifs. Surprisingly, the structure reveals a novel metal binding site composed of residues conserved in most lipid kinases. | |
650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinsk bioteknologix Medicinsk bioteknologi0 (SwePub)304012 hsv//swe |
650 | 7 | a MEDICAL AND HEALTH SCIENCESx Medical Biotechnologyx Medical Biotechnology0 (SwePub)304012 hsv//eng |
653 | a Biochemistry | |
653 | a Biokemi | |
700 | 1 | a Herman, Maria Dolores4 aut |
700 | 1 | a Johnson, Kenneth A.4 aut |
700 | 1 | a Kelly, Amélie A.4 aut |
700 | 1 | a Wieslander, Åkeu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)awies |
700 | 1 | a Hallberg, B. M.u Karolinska Institutet4 aut |
700 | 1 | a Nordlund, Päru Karolinska Institutet4 aut |
710 | 2 | a Stockholms universitetb Institutionen för biokemi och biofysik4 org |
773 | 0 | t Journal of Biological Chemistryg 282:27, s. 19644-19652q 282:27<19644-19652x 0021-9258x 1083-351X |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-25485 |
856 | 4 8 | u https://doi.org/10.1074/jbc.M604852200 |
856 | 4 8 | u http://kipublications.ki.se/Default.aspx?queryparsed=id:115585103 |
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