| Type: | Domain | Name: | Ribonuclease A-domain |
| Description: | Pancreatic ribonucleases (RNaseA) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and ofsome reptiles []. Specifically, the enzymes are involved in endonucleolyticcleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. Ribonuclease canunwind the DNA helix by complexing with single-stranded DNA; the complex arises by an extended multi-site cation-anion interaction between lysineand arginine residues of the enzyme and phosphate groups of the nucleotides. Other proteins belonging to the pancreatic RNAse family include: bovineseminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases []; liver-type ribonucleases []; angiogenin, which induces vascularisationof normal and malignant tissues; eosinophil cationic protein [], acytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin.The sequence of pancreatic RNases contains four conserved disulphide bonds and three amino acid residues involved in the catalytic activity.This entry represents a domain in Ribonuclease A. Its structure is an alpha+beta fold -- long curved beta sheet and three helices. | Short Name: | RNaseA_domain |
