Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8)of triosephosphate isomerase: Toward a new substrate specificity

Proteins: Structure, Function and Genetics

Volumn 42, Issue 3, 2001, Pages 383-389

  Norledge, Brian V ^a   Lambeir, Anne M ^b   Abagyan, Ruben A ^c   Rottmann, Antje ^d   Fernandez, Anna M ^e   Filimonov Martin, Vladimir V ^f   Peter, G ^a   Wierenga, Rik K ^a  

^a UNIVERSITY OF OULU   (Finland)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c UNIVERSITY OF ANTWERP   (Belgium)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

^e UNIVERSITY OF POTSDAM   (Germany)

^f UNIVERSITY OF GRANADA   (Spain)

Author keywords

Folding intermediate; Folding pathway; Loop modeling; Protein design; Triosephosphate isomerase (TIM)

Indexed keywords

DIHYDROXYACETONE PHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE; MUTANT PROTEIN; PHOSPHATE BINDING AGENT; PROTOZOAL PROTEIN; TRIOSEPHOSPHATE ISOMERASE;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; EVOLUTION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRUCTURE ANALYSIS; TRYPANOSOMA; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLIZATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PHOSPHATES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TRIOSE-PHOSPHATE ISOMERASE;

EID: 0035865949     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0134(20010215)42:3<383::AID-PROT80>3.0.CO;2-G     Document Type: Article

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