Literature summary for 2.4.1.68 extracted from

Ihara, H.; Okada, T.; Taniguchi, N.; Ikeda, Y.
Involvement of the alpha-helical and Src homology 3 domains in the molecular assembly and enzymatic activity of human alpha1,6-fucosyltransferase, FUT8 (2020), Biochim. Biophys. Acta, 1864, 129596 .

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Sf21 and in COS-1cell	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular modeling predicts homophilic dimerization. Residues Ala123, Leu130, and Leu137 of alpha1-helix, and Ala149, Leu156, Ile163, Leu170 of the alpha2-helix all contribute to the formation of the hydrophobic core in the four alpha-helices bundle. The bundle is formed via intermolecular and intramolecular hydrophobic interactions and provides an interface for other intermolecular interactions. In the prediction, each of the SH3 domains is located in close proximity to the interface formed by the alpha-helical domain of the counterpart in the predicted dimer	Homo sapiens

Crystallization (Comment)

Organism

molecular modeling predicts homophilic dimerization. Residues Ala123, Leu130, and Leu137 of alpha1-helix, and Ala149, Leu156, Ile163, Leu170 of the alpha2-helix all contribute to the formation of the hydrophobic core in the four alpha-helices bundle. The bundle is formed via intermolecular and intramolecular hydrophobic interactions and provides an interface for other intermolecular interactions. In the prediction, each of the SH3 domains is located in close proximity to the interface formed by the alpha-helical domain of the counterpart in the predicted dimer

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D32C	mutation introduces covalent dimerization, activity is similar to wild-type	Homo sapiens
additional information	the N-terminal alpha-helical domain is required for the full activity. The deletion of residues 1-67 and residues 1-108 has no effect on the activity. Further deletion results in the loss of activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BYC5	-	-

General Information

General Information	Comment	Organism
physiological function	FUT8 potentially forms homodimers in vivo via intermolecular hydrophobic interactions involving alpha-helical domains. alpha-Helical and SH3 domains are all required for enzymatic activity. The SH3 domain locates in close proximity to the alpha-helical domain in an intermolecular manner	Homo sapiens