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In this work, we develop first near-complete 3D models for NTD-hXPB - theN-terminal protein domain of the human transcription factor XPB. The resultsare very significant as NTD-hXPB plays a critical role in the synthesis ofproteins (specifically transcription) and DNA damage repair (specificallynucleotide excision repair). NTD-hXPB is directly implicated in rare diseasesXP-B, XP-CS, and TTD2, whose symptoms include neurodegenerative disorders,premature aging, and decreased fertility. NTDhXPB is also linked to anti-cancertherapies. As a bi-product we derived 3D models of NTD-mXPB - homologue ofNTD-hXPB in mycobacterium tuberculosis aka MTB (causative agent of most casesof tuberculosis, which surpassed HIV as #1 infectious disease killer in 2014).These could be potential target for TB therapeutics. Our ab-initio modellingprotocol takes advantage of recent powerful advances (prediction of contactresidues) in protein structure modeling. Our protocol also includes human inthe loop, inspired by the prevailing theory that computational abilities ofhuman minds can be powerfully harnessed in engineering/problem-solving. Usingthe developed models in this paper, we are able to propose significant insightsinto (a) the role of NTD-hXPB in the process of transcription and DNA damagerepair (specifically NER), (b) the critical interactions of NTD-hXPB withanother co-labourer protein p52, (c) diseases associated with NTD-hXPB, and (d)alterations in functionalities between NTD-hXPB (in human) and NTD-mXPB (in TBpathogen).

Modelling the Structure of a Protein Domain (N-terminal of XPB) Linked  with Protein Synthesis, DNA Damage Repair, Rare Diseases, Cancer  Therapeutics, and Tuberculosis