The histamine N-methyltransferase T1051 polymorphism affects active site structure and dynamics

Biochemistry

Volumn 47, Issue 3, 2008, Pages 893-901

  Rutherford, Karen ^a   Parson, W W ^a   Daggett, Valerie ^a,b  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b University of Washington   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BRAIN; COMPUTER SIMULATION; CRYSTAL STRUCTURE; ENZYMES; MAMMALS; MOLECULAR DYNAMICS;

ACTIVE SITE STRUCTURES; BREATHING MOTION; HISTAMINES;

POLYMORPHISM;

ENZYME VARIANT; HISTAMINE; HISTAMINE METHYLTRANSFERASE; ISOLEUCINE; THREONINE;

ALPHA HELIX; ARTICLE; BETA SHEET; BINDING SITE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME POLYMORPHISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GENE; HNMT GENE; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; SIMULATION;

CATALYTIC DOMAIN; COMPUTER SIMULATION; HISTAMINE; HISTAMINE N-METHYLTRANSFERASE; HUMANS; HYDROPHOBICITY; MODELS, MOLECULAR; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; S-ADENOSYLMETHIONINE; WATER;

MAMMALIA;

EID: 38349189694     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701737f     Document Type: Article

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