Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution.

Article Details

Citation

Pous J, Mallorqui-Fernandez G, Peracaula R, Terzyan SS, Futami J, Tada H, Yamada H, Seno M, de Llorens R, Gomis-Ruth FX, Coll M

Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution.

Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):498-505.

PubMed ID
11264578 [ View in PubMed
]
Abstract

Human pancreatic ribonuclease 1 (RNase 1) is considered to be the human counterpart of bovine pancreatic RNase A. Truncation of seven amino-acid residues from the amino-terminal sequence resulted in RNase 1 Delta N7, which has a reduced ribonucleolytic activity and a lower affinity for the human placental RNase inhibitor (PRI). This RNase 1 variant has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data to 1.9 A resolution. The molecule displays the alpha + beta folding topology typical of members of the RNase A superfamily. The main distinct features found in RNase 1 Delta N7 are basically located in three loops affecting the fitting of the enzyme to the active site of subtilisin and the shape of the B2 subsite. These changes, taken with the lack of the catalytically active residue Lys7, may explain the reduced affinity of RNase 1 Delta N7 for PRI and the low ribonucleolytic activity of the protein when compared with the native enzyme.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Ribonuclease pancreaticP07998Details