XPD Helicase (3CRV): Difference between revisions

XPD helicase is made up of alpha helices and beta sheets and contains one main domain, a DNA interaction interface. There are two motifs, one of which performs the function of unwinding the DNA strand. The second motif, located at residues 682-695, directs XPD helicase to the nucleus, as it is the nuclear localization signal. Residues 7-283 form the Helicase ATP binding domain(<scene name='72/728075/Binding_domain/5'>Helicase-ATP Domain</scene>), where ATP itself binds at residues 42-49, (<scene name='72/728075/Nucleotide_binding/4'>ATP Binding</scene>). Interaction with the gene MMS19 is mediated by region consisting of residues 438-637. Residues 234-237 form the motif which is the DEAH box of this transcription factor which is where the unwinding of DNA is performed (<scene name='72/728075/Deah_box/1'>DEAH Box</scene>). Iron Sulfur bonding residues consist of C116, C134, C155, and C160,(<scene name='72/728075/Iron_sulfur/1'>Iron Sulfur Binding</scene>). Features of Cockayne Syndrome and Xeroderma pigmentosum  have been associated with the point mutation G602D, and the point mutation L461V is associated with TTD1 <ref>DOI 10.1093/nar/gku989 </ref>.