The V119I polymorphism in protein L-isoaspartate O-methyltransferase alters the substrate-binding interface

Protein Engineering, Design and Selection

Volumn 22, Issue 12, 2009, Pages 713-721

  Rutherford, Karen ^a,c   Daggett, Valerie ^a,b  

^a Department of Biochemistry ^*  (United States)

^b University of Washington   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Aging; Molecular dynamics; Polymorphisms; Protein isoaspartate O methyltransferase; Protein repair

Indexed keywords

ACTIVE SITE; AGING; BINDING AND RELEASE; BRIDGE NETWORKS; CO-SUBSTRATE; DOCKING SITES; HETEROZYGOSITY; METHYLATION REACTION; MOLECULAR BASIS; MOLECULAR DYNAMICS SIMULATIONS; O-METHYLTRANSFERASE; S-ADENOSYLMETHIONINE; SIDE-CHAIN INTERACTIONS; SUBSTRATE-BINDING; SUBSTRATE-BINDING SITES; THERMAL STABILITY;

ALKYLATION; BINDING ENERGY; ENZYMES; FORESTRY; METHYLATION; MOLECULAR DYNAMICS; POLYMORPHISM; PROTEINS; REACTION KINETICS; REPAIR; SUBSTRATES;

BINDING SITES;

ISOASPARTATE O METHYLTRANSFERASE; METHYLTRANSFERASE; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

ALLELE; ARTICLE; BINDING SITE; HUMAN; METHYLATION; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN POLYMORPHISM; THERMOSTABILITY;

MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; POLYMORPHISM, GENETIC; PROTEIN CONFORMATION; PROTEIN D-ASPARTATE-L-ISOASPARTATE METHYLTRANSFERASE; SUBSTRATE SPECIFICITY;

EID: 72649084172     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzp056     Document Type: Article

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