The highly refined solution structure of the cytotoxic ribonuclease α-Sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity

Journal of Molecular Biology

Volumn 299, Issue 4, 2000, Pages 1061-1073

  Pérez Cañadillas, José Manuel ^a   Santoro, Jorge ^a   Campos Olivas, Ramón ^a   Lacadena, Javier ^b   Martínez Del Pozo, Alvaro ^b   Gavilanes, José G ^b   Rico, Manuel ^a   Bruix, Marta ^a  

^a INSTITUTO DE ESTRUCTURA DE LA MATERIA   (Spain)

^b UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

Author keywords

NMR solution structure; Protein RNA interaction; Ribonucleolytic activity; Ribosome inactivating protein; sarcin

Indexed keywords

ALPHA SARCIN; RESTRICTOCIN; RIBONUCLEASE; RIBOSOME INACTIVATING PROTEIN; RIBOSOME RNA; RICIN;

ARTICLE; ASPERGILLUS; ASPERGILLUS GIGANTEUS; CHEMICAL BOND; CONTROLLED STUDY; CYTOTOXICITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; RIBOSOME; RNA SEQUENCE;

EID: 0034674158     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3813     Document Type: Article

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