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Volumn 278, Issue 16, 2003, Pages 14420-14428
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Crystal structure of an α1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
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Author keywords
[No Author keywords available]
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Indexed keywords
BIOSYNTHESIS;
CATALYSIS;
CRYSTAL STRUCTURE;
GENES;
SUBSTRATES;
X RAY ANALYSIS;
TRANSFER REACTIONS;
BIOCHEMISTRY;
ALPHA1,4 N ACETYLHEXOSAMINYLTRANSFERASE;
ASPARAGINE;
GLUCURONIC ACID;
GLYCOSAMINOGLYCAN;
HEPARAN SULFATE;
N ACETYLGALACTOSAMINE;
N ACETYLGLUCOSAMINE;
UNCLASSIFIED DRUG;
URIDINE DIPHOSPHATE;
URIDINE DIPHOSPHATE N ACETYLGALACTOSAMINE;
URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;
ARGININE;
ASPARTIC ACID;
EXTL2 PROTEIN, HUMAN;
MEMBRANE PROTEIN;
N ACETYLGALACTOSAMINYLTRANSFERASE;
N ACETYLGLUCOSAMINYLTRANSFERASE;
UDP N ACETYLGALACTOSAMINE (GLCUA GALNAC 4 SULFATE)(4) N ACETYLGALACTOSAMINYLTRANSFERASE;
UDP-N-ACETYLGALACTOSAMINE (GLCUA-GALNAC-4-SULFATE)(4) N-ACETYLGALACTOSAMINYLTRANSFERASE;
ANIMAL CELL;
ARTICLE;
BIOSYNTHESIS;
CATALYSIS;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME STRUCTURE;
EXOSTOSIN GENE;
GENE;
MOUSE;
MULTIGENE FAMILY;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PRIORITY JOURNAL;
SITE DIRECTED MUTAGENESIS;
AMINO ACID SEQUENCE;
ANIMAL;
BINDING SITE;
CELL STRAIN COS1;
CHEMICAL STRUCTURE;
CHEMISTRY;
GENETIC TRANSFECTION;
HYDROGEN BOND;
METABOLISM;
MOLECULAR GENETICS;
PROTEIN CONFORMATION;
PROTEIN TERTIARY STRUCTURE;
SEQUENCE HOMOLOGY;
X RAY CRYSTALLOGRAPHY;
ANIMALIA;
AMINO ACID SEQUENCE;
ANIMALS;
ARGININE;
ASPARAGINE;
ASPARTIC ACID;
BINDING SITES;
CATALYTIC DOMAIN;
COS CELLS;
CRYSTALLOGRAPHY, X-RAY;
HEPARITIN SULFATE;
HYDROGEN BONDING;
MEMBRANE PROTEINS;
MICE;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
N-ACETYLGALACTOSAMINYLTRANSFERASES;
N-ACETYLGLUCOSAMINYLTRANSFERASES;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
TRANSFECTION;
URIDINE DIPHOSPHATE N-ACETYLGLUCOSAMINE;
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EID: 0012784535
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M210532200 Document Type: Article |
Times cited : (93)
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References (27)
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