X-ray Structure for an RNase H Inhibitor Bound to HIV-1 Reverse Transcriptase

摘要: The proteins of the Nuclear Factor-kappaB (NF-țB) family proteins are important transcription factors that regulate the expression of genes involved in immune and inflammatory response and apoptosis. There are five known NF-țB proteins, p50 (NF-țB1), p52 (NF-țB2), p65 (RelA), c-Rel and RelB, that exist as homo-and heterodimers. Unlike other family members that form all possible functional combinatorial dimers, RelB forms heterodimers with only p100/p52 and p105/p50. The X-ray crystal structure of the RelB dimerization domain (DD) alone, and in complex with p52 DD have been determined. This reveals that RelB/p52 DD heterodimer forms a “regular” dimer similar to other NF-țB dimers, unlike RelB DD which forms an intertwined homodimer. We have shown that RelB forms an intertwined homodimer in solution as well. The residues that are critical in NF-țB dimer formation are invariant in RelB …