Mutational Analysis of residue V408 of LEDGE/p75

B, Keerthana (2016) Mutational Analysis of residue V408 of LEDGE/p75. Masters thesis, Indian Institute of Technology Hyderabad.

[img] Text
BO14MTECH11001.pdf - Submitted Version
Restricted to Registered users only until 1 July 2019.

Download (1MB) | Request a copy

Abstract

Lens Epithelium Derived Growth Factor (LEDGF/p75) is a human transcriptional co-activator and a dominant cellular binding partner of HIV-1 Integrase (IN). LEDGF/p75 tethers IN to the host chromatin aiding in formation of proviral DNA. This study involves generation of site directed mutations of Valine residue at position 408 and analyzing the effect of mutation upon interaction with IN. Previously characterized mutations L368A and D366A have been generated for serving as controls in pull-down analysis. The binding affinity of V408 and L368 mutants will be characterized by pull down analysis.

[error in script]
IITH Creators:
IITH CreatorsORCiD
Item Type: Thesis (Masters)
Uncontrolled Keywords: LEDGF, P75, V408, TD586
Subjects: Others > Biotechnology
Divisions: Department of Biotechnology
Depositing User: Library Staff
Date Deposited: 12 Jul 2016 04:49
Last Modified: 12 Jul 2016 04:49
URI: http://raiith.iith.ac.in/id/eprint/2523
Publisher URL:
Related URLs:

Actions (login required)

View Item View Item
Statistics for RAIITH ePrint 2523 Statistics for this ePrint Item