Literature summary for 3.1.6.13 extracted from

Saito, S.; Ohno, K.; Okuyama, T.; Sakuraba, H.
Structural basis of mucopolysaccharidosis type II and construction of a database of mutant iduronate 2-sulfatases (2016), PLoS ONE, 11, e0163964 .

Application

Application	Comment	Organism
medicine	structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations identified in patients with mucopolysaccharidosis MPS II. The amino acid substitutions causing MPS II are widely spread over the enzyme molecule and the structural changes of the enzyme protein are generally larger in the severe group than in the attenuated one. The structural changes influence the disease progression	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations identified in patients with mucopolysaccharidosis MPS II. The amino acid substitutions causing MPS II are widely spread over the enzyme molecule and the structural changes of the enzyme protein are generally larger in the severe group than in the attenuated one. The structural changes influence the disease progression	Homo sapiens

Crystallization (Comment)

Organism

structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations identified in patients with mucopolysaccharidosis MPS II. The amino acid substitutions causing MPS II are widely spread over the enzyme molecule and the structural changes of the enzyme protein are generally larger in the severe group than in the attenuated one. The structural changes influence the disease progression

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P22304	-	-

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Release 2023.1 (January 2023)