Madhusudhan, MS and Vishveshwara, S (1998) Modeling of angiogenin-3 '-NMP complex. In: Journal of Biomolecular Structure & Dynamics, 16 (3). pp. 715-722.
Full text not available from this repository. (Request a copy)Abstract
Angiogenin belongs to the Ribonuclease superfamily and has a weak enzymatic activity that is crucial for its biological function of stimulating blood vessel growth. Structural studies on ligand bound Angiogenin will go a long way in understanding the mechanism of the protein as well as help in designing drugs against it. In this study we present the first available structure of nucleotide ligand bound Angiogenin obtained by computer modeling. The importance of this study in itself notwithstanding, is a precursor to modeling a full dinucleotide substrate onto Angiogenin. Bovine Angiogenin, the structure of which has been solved at a high resolution, was earlier subjected to Molecular Dynamics simulations for a nanosecond. The MD structures offer better starting points for docking as they offer lesser obstruction than the crystal structure to ligand binding. The MD structure with the least serious short contacts was modeled to obtain a steric free Angiogenin - 3' mononucleotide complex structure. The structures were energetically minimized and subjected to a brief spell of Molecular Dynamics. The results of the simulation show that all the li,ligand-Angiogenin interactions and hydrogen bonds are retained, redeeming the structure and docking procedure. Further, following ligand - protein interactions in the case of the ligands 3'-CMP and 3'-UMP we were able to speculate on how Angiogenin, a predominantly prymidine specific ribonuclease prefers Cytosine to Uracil in the first base position.
| Item Type: | Journal Article |
|---|---|
| Publication: | Journal of Biomolecular Structure & Dynamics |
| Publisher: | Adenine Press |
| Additional Information: | Copyright of this article belongs to Adenine Press. |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 09 Jun 2011 06:32 |
| Last Modified: | 09 Jun 2011 06:32 |
| URI: | http://eprints.iisc.ac.in/id/eprint/38169 |
Actions (login required)
 |
View Item |
