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Mevalonate kinase
From Proteopedia
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| - | <StructureSection load='2hfu' size='340' side='right' caption=' | + | <StructureSection load='2hfu' size='340' side='right' caption='Mevalonate kinase complex with mevalonate (PDB code [[2hfu]]).' scene=''> |
__TOC__ | __TOC__ | ||
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== Structural highlights == | == Structural highlights == | ||
| + | The 3D structure of MK complex with mevalonate shows the enzyme composed of 2 domains: The N-terminal and the C-terminal. The mevalonate binds in a deep cleft between the 2 domains forming H-bond interactions with Arg and Tyr residues and several hydrophobic interactions<ref>PMID:17397541</ref>. | ||
==3D structures of mevalonate kinase== | ==3D structures of mevalonate kinase== | ||
Revision as of 06:47, 13 October 2020
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References
- ↑ Buhaescu I, Izzedine H. Mevalonate pathway: a review of clinical and therapeutical implications. Clin Biochem. 2007 Jun;40(9-10):575-84. doi: 10.1016/j.clinbiochem.2007.03.016., Epub 2007 Mar 31. PMID:17467679 doi:http://dx.doi.org/10.1016/j.clinbiochem.2007.03.016
- ↑ Levy M, Arion A, Berrebi D, Cuisset L, Jeanne-Pasquier C, Bader-Meunier B, Jung C. Severe early-onset colitis revealing mevalonate kinase deficiency. Pediatrics. 2013 Sep;132(3):e779-83. doi: 10.1542/peds.2012-3344. Epub 2013 Aug, 26. PMID:23979089 doi:http://dx.doi.org/10.1542/peds.2012-3344
- ↑ Sgraja T, Smith TK, Hunter WN. Structure, substrate recognition and reactivity of Leishmania major mevalonate kinase. BMC Struct Biol. 2007 Mar 30;7:20. PMID:17397541 doi:10.1186/1472-6807-7-20
