Structure-based protein engineering efforts with a monomeric TIM variant: The importance of a single point mutation for generating an active site with suitable binding properties

Protein Engineering, Design and Selection

Volumn 21, Issue 4, 2008, Pages 257-266

  Alahuhta, Markus ^a   Salin, Mikko ^a   Casteleijn, Marco G ^a   Kemmer, Christian ^a   El Sayed, Ibrahim ^b   Augustyns, Koen ^b   Neubauer, Peter ^a   Wierenga, Rik K ^a  

^a UNIVERSITY OF OULU   (Finland)

^b UNIVERSITY OF ANTWERP   (Belgium)

Author keywords

Citrate; Monomeric TIM; Protein design; Suicide inhibitor; Transition state analog

Indexed keywords

BIOCHEMISTRY; CHEMICAL BONDS; PHOSPHATES; SUBSTRATES;

PROTEIN DESIGN; SUICIDE INHIBITORS; TRANSITION STATE ANALOG;

PROTEINS;

CITRIC ACID; PHOSPHATE; TRIOSEPHOSPHATE ISOMERASE;

ANALYTIC METHOD; ARTICLE; BINDING SITE; CORRELATION ANALYSIS; GEOMETRY; HYDROGEN BOND; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN ENGINEERING; WILD TYPE;

ACETONE; BINDING SITES; CATALYSIS; CITRIC ACID; CRYSTALLOGRAPHY, X-RAY; GLUTAMIC ACID; MODELS, MOLECULAR; MUTANT PROTEINS; POINT MUTATION; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; TRIOSE-PHOSPHATE ISOMERASE;

EID: 41149102837     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzn002     Document Type: Article

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