title: Structure of an RNase-related protein from Calystegia sepium.
abstract: The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical alpha + beta structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the 'active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
authors.affiliation: Laboratory of Analytical Chemistry and Medicinal Physicochemistry, Faculty of Pharmaceutical Sciences, K. U. Leuven, E. Van Evenstraat 4, B-3000 Leuven, Belgium.
authors.forename: A
authors.initials: A
authors.lastname: Rabijns
authors.forename: C
authors.initials: C
authors.lastname: Verboven
authors.forename: P
authors.initials: P
authors.lastname: Rougé
authors.forename: A
authors.initials: A
authors.lastname: Barre
authors.forename: E J M
authors.initials: EJ
authors.lastname: Van Damme
authors.forename: W J
authors.initials: WJ
authors.lastname: Peumans
authors.forename: C J
authors.initials: CJ
authors.lastname: De Ranter
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
chemical_list: D010940:Plant Proteins; C405543:RNase-related protein, Calystegia sepium