Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation

Nature Communications

Volumn 6, Issue , 2015, Pages

  Lira Navarrete, Erandi ^a   De Las Rivas, Matilde ^a   Compañón, Ismael ^b   Pallarés, María Carmen ^a   Kong, Yun ^c   Iglesias Fernández, Javier ^d,j   Bernardes, Gonçalo J L ^e,f   Peregrina, Jesús M ^b   Rovira, Carme ^d,g   Bernadó, Pau ^h   Bruscolini, Pierpaolo ^a   Clausen, Henrik ^c   Lostao, Anabel ^a,i   Corzana, Francisco ^b   Hurtado Guerrero, Ramon ^a,i  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b UNIVERSITY OF LA RIOJA   (Spain)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

^d UNIVERSITY OF BARCELONA   (Spain)

^e UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^f INSTITUTO DE MEDICINA MOLECULAR   (Portugal)

^g INSTITUCIÓ CATALANA DE RECERCA I ESTUDIS AVANÇATS ICREA   (Spain)

^h INSERM   (France)

ⁱ FUNDACIÓN ARAID   (Spain)

^j KING'S COLLEGE LONDON   (United Kingdom)

more..

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; LECTIN; MANGANESE; MONOMER; MUCIN 5AC; N ACETYLGALACTOSAMINYLTRANSFERASE; SUGAR NUCLEOTIDE; URIDINE DIPHOSPHATE; NUCLEOTIDE; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE;

CATALYSIS; CHEMICAL BINDING; CRYSTAL STRUCTURE; ENZYME ACTIVITY; HETEROGENEITY; MOLECULAR ANALYSIS; PROTEIN; SCATTERING;

ARTICLE; ATOMIC FORCE MICROSCOPY; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HYDROGEN BOND; MOLECULAR DYNAMICS; NUCLEOTIDE BINDING SITE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN GLYCOSYLATION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY; CHEMISTRY; ENZYME SPECIFICITY; GLYCOSYLATION; METABOLISM; MOLECULAR MODEL; STRUCTURE ACTIVITY RELATION;

CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLYCOPEPTIDES; GLYCOSYLATION; LECTINS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; N-ACETYLGALACTOSAMINYLTRANSFERASES; NUCLEOTIDES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84929208855     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7937     Document Type: Article

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