Structural highlights
Function
[ANG1_BOVIN] May function as a tRNA-specific ribonuclease that abolishes protein synthesis by specifically hydrolyzing cellular tRNAs. Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo. Has very low ribonuclease activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of bovine angiogenin has been determined using two- and three-dimensional proton NMR spectroscopy. The solution structure is very close to that recently determined by X-ray diffraction analysis. This structure appears well defined, even if five loops and one helix exhibit greater flexibility. Analysis of the active site geometry confirms the position of the Glu-118 residue which obstructs the pyrimidine binding site. There is no experimental evidence of an unobstructed conformation of angiogenin in solution. In addition, it appears that the Glu-118 and Ser-119 residues and the cell receptor binding loop may play an important role in the differences of C-terminal fragment organization and ribonucleolytic activity observed between angiogenins and ribonuclease A.
Solution structure of bovine angiogenin by 1H nuclear magnetic resonance spectroscopy.,Lequin O, Albaret C, Bontems F, Spik G, Lallemand JY Biochemistry. 1996 Jul 9;35(27):8870-80. PMID:8688423[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lequin O, Albaret C, Bontems F, Spik G, Lallemand JY. Solution structure of bovine angiogenin by 1H nuclear magnetic resonance spectroscopy. Biochemistry. 1996 Jul 9;35(27):8870-80. PMID:8688423 doi:http://dx.doi.org/10.1021/bi960022r
