ASF1 like histone chaperone
| ASF1_hist_chap | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the cia- histone h3-h4 complex | |||||||||
| Identifiers | |||||||||
| Symbol | ASF1_hist_chap | ||||||||
| Pfam | PF04729 | ||||||||
| Pfam clan | CL0463 | ||||||||
| InterPro | IPR006818 | ||||||||
| SCOP | 1roc | ||||||||
| SUPERFAMILY | 1roc | ||||||||
| |||||||||
In molecular biology, the ASF1 like histone chaperone family of proteins includes the yeast and human ASF1 proteins. These proteins have histone chaperone activity.[1] ASF1 participates in both the replication-dependent and replication-independent pathways. The three-dimensional structure has been determined as a compact immunoglobulin-like beta sandwich fold topped by three helical linkers.[2]
References
- ↑ Daganzo SM, Erzberger JP, Lam WM, Skordalakes E, Zhang R, Franco AA, Brill SJ, Adams PD, Berger JM, Kaufman PD (December 2003). "Structure and function of the conserved core of histone deposition protein Asf1". Curr. Biol. 13 (24): 2148–58. doi:10.1016/j.cub.2003.11.027. PMID 14680630.
- ↑ Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M (March 2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes Cells 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID 10759893.
This article incorporates text from the public domain Pfam and InterPro IPR006818
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