International Journal of Science and Research (IJSR)

International Journal of Science and Research (IJSR)
Call for Papers | Fully Refereed | Open Access | Double Blind Peer Reviewed

ISSN: 2319-7064


Downloads: 134 | Views: 190

Research Paper | Biology | India | Volume 5 Issue 3, March 2016


Molecular Docking Studies of Human Ubiquitin Conjugating Enzyme Rad6: A Systematic in Silico Approach

Dhafir Latief Fayadh | Dr. K. Venkateswara Swamy


Abstract: This study confirms the ubiquitin conjugating enzyme 2B (Rad6) plays a significant role in the DNA repair pathway also because the ubiquitin-conjugating pathway. The DNA repair pathway could be a variety of bypass repair mechanism where the broken base pair is bypassed by permitting the replication fork to labor under the site of injury. This is often done by a shift mechanism wherever deoxyribonucleic acid enzyme - ? is switched with DNA enzyme - ? (DNAP - ?). Site of DNAP - ? is massive enough to permit the broken ester to labor under, and so bypass the broken nucleotide. However, this is often potential solely through the involvement of Proliferating cell nuclear antigen (PCNA) that could be a processivity issue and it acts as a platform for the achievement of DNAP - ?. Once the DNAP - ? is recruited, the DNA bypass mechanism is initiated. PCNA is activated by ubiquitination of essential amino acid residue by Rad6-Rad18 advanced. Once Rad6 is ubiquitylated, it forms complex with Rad18 and this complex then ubiquitylated PCNA, that successively initiates error-free DNA bypass repair. Typically, attributable to exposure to radiation the Rad6-Rad18 advanced is not shaped. Within the absence of Rad6-Rad18 advanced, PCNA isn't activated and DNAP - ? isn't recruited at the harm the site. Therefore, deoxyribonucleic acid bypass mechanism isn't initiated. We tend to intend the activation of Rad6 by the triazole compounds to make a complex with Rad18 and ubiquitination of PCNA to initiate deoxyribonucleic acid bypass repair.


Keywords: molecular docking, human ubiquitin conjugating enzyme Rad6, in silico


Edition: Volume 5 Issue 3, March 2016,


Pages: 636 - 641


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