Primary citation
Title Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
Authors Kemmink,; Darby,; Dijkstra,; Nilges,; Creighton,
Journal BIOCHEMISTRYsearch vol:35, pag:7684-7691 (1996), Identifiers: PubMed ID (8672469)search DOI (10.1021/bi960335m)
Abstract As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization.
MeSH terms Amino Acid Sequencesearch, Carbon Isotopessearch, Cloningsearch, Molecularsearch, Computer Simulationsearch, Escherichia colisearch, Humanssearch, Isomerasessearch, Magnetic Resonance Spectroscopysearch, Modelssearch, Molecularsearch, Modelssearch, Structuralsearch, Molecular Sequence Datasearch, Nitrogen Isotopessearch, Protein Conformationsearch, Protein Disulfide-Isomerasessearch, Recombinant Proteinssearch, Sequence Homologysearch, Amino Acidsearch, Softwaresearch, Thioredoxinssearch
Secondary citations
Title Nuclear Magnetic Resonance Characterization of the N-Terminal Thioredoxin-Like Domain of Protein Disulfide Isomerase
Authors Kemmink,; Darby,; Dijkstra,; Scheek,; Creighton,
Journal PROTEIN vol:4, pag:2587 (1995)