Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite

Proceedings of the National Academy of Sciences of the United States of America

Volumn 115, Issue 18, 2018, Pages 4637-4642

  Kadirvelraj, Renuka ^a   Yang, Jeong Yeh ^b   Sanders, Justin H ^a   Liu, Lin ^b   Ramiah, Annapoorani ^b   Prabhakar, Pradeep Kumar ^b   Boons, Geert Jan ^b   Wood, Zachary A ^a   Moremen, Kelley W ^a,b  

^a University of Georgia ^*  (United States)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

Convergent evolution; Exosite; Glycosyltranferase; N glycan processing; Substrate recognition

Indexed keywords

ALPHA MANNOSIDASE II; ASPARAGINE; GLYCOSIDASE; GLYCOSYLTRANSFERASE; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINYLTRANSFERASE II; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; ALPHA-1,6-MANNOSYL-GLYCOPROTEIN BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE; N ACETYLGLUCOSAMINYLTRANSFERASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; EMBRYO; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN FOLDING; CHEMISTRY; METABOLISM; PROTEIN DOMAIN;

HUMANS; N-ACETYLGLUCOSAMINYLTRANSFERASES; PROTEIN DOMAINS; PROTEIN FOLDING; URIDINE DIPHOSPHATE N-ACETYLGLUCOSAMINE;

EID: 85046261666     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1716988115     Document Type: Article

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