A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III.
Leulliot, Nicolas
A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III. [electronic resource] - The EMBO journal Jul 2004 - 2468-77 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0261-4189
10.1038/sj.emboj.7600260 doi
Amino Acid Sequence
Base Sequence
Catalytic Domain
Crystallography, X-Ray
Fungal Proteins--chemistry
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Nucleic Acid Conformation
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
RNA, Double-Stranded--metabolism
RNA, Fungal--chemistry
Ribonuclease III--chemistry
Saccharomyces cerevisiae--metabolism
Saccharomyces cerevisiae Proteins--chemistry
Sequence Homology, Amino Acid
Solutions
Substrate Specificity
A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III. [electronic resource] - The EMBO journal Jul 2004 - 2468-77 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0261-4189
10.1038/sj.emboj.7600260 doi
Amino Acid Sequence
Base Sequence
Catalytic Domain
Crystallography, X-Ray
Fungal Proteins--chemistry
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Nucleic Acid Conformation
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
RNA, Double-Stranded--metabolism
RNA, Fungal--chemistry
Ribonuclease III--chemistry
Saccharomyces cerevisiae--metabolism
Saccharomyces cerevisiae Proteins--chemistry
Sequence Homology, Amino Acid
Solutions
Substrate Specificity