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histone fold
A histone fold is a structurally conserved motif found near the C-terminus in every core histone sequence in a histone octamer responsible for the binding of histones into heterodimers.
The histone fold averages about 70 amino acids and consists of three alpha helices connected by two short, unstructured loops.〔Alva, V., Ammelburg, M., Soding, J. & Lupas, A.N. (2007). On the origin of the histone fold. BioMed Central Structural Biology. 7(17). doi: 10.1186/1472-6807-7-17〕 When not in the presence of DNA, the core histones assemble into head-to-tail intermediates (H3 and H4 first assemble into heterodimers then fuse two heterodimers to form a tetramer, while H2A and H2B form heterodimers〔Watson et al. (2007). Molecular biology of the gene. Benjamin Cummings. pp. 224〕) via extensive hydrophobic interactions between each histone fold domain in a "handshake motif".〔Arrents, G. & Mourdrianakis, E.N. (1995). The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization. PNAS. 92, 11170-11174. Retrieved from http://www.pnas.org/content/92/24/11170.full.pdf〕
==References==
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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