id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_s6wc3ukn2zbptprjt4a77pnoxy	Arnthor Ævarsson	Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease	2000	15	.pdf	application/pdf	11587	957	64	Crystal structure of human branched-chain αα-ketoacid determined the crystal structure of branched-chain α-ketoacid dehydrogenase MSUD mutations affect the catalysis, folding and assembly of this clinically important protein. and activity of the branched-chain dehydrogenase multienzyme complex from rat liver is to a large extent dependent on the presence of K+ with the E1 component being The K+ bound at site 1 (Figure 3b) stabilizes a loop containing residues 161–166 of the α subunit. substrate binding due to these mutations, it is not surprising that this causes the classic severe type of MSUD. well with the relatively small predicted effect of the mutations on protein structure and stability. Missense mutations in E1b subunits and clinical phenotypes of MSUD patients. MSUD mutations affecting cofactor binding MSUD mutations affecting subunit interactions. (a) Mutations in the small C-terminal domain of the α subunit at the mutations in the human E1b subunit of branched chain α-ketoacid	./cache/work_s6wc3ukn2zbptprjt4a77pnoxy.pdf	./txt/work_s6wc3ukn2zbptprjt4a77pnoxy.txt