Structural highlights
Function
ARI3A_HUMAN Transcription factor which may be involved in the control of cell cycle progression by the RB1/E2F1 pathway and in B-cell differentiation.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The AT-rich interactive domain (ARID) of human AT-rich interactive domain-containing protein 3A (ARID3A) has been selected for structural characterization by Northeast Structural Genomics Consortium (residues 218-351 NESG ID HR4394C) as part of our Human Cancer Protein Interaction Network (HCPIN) project. Protein ARID3A belongs to the ARID family DNA-binding protein and is known to play important roles in embryonic patterning, cell lineage gene regulation, and cell cycle control, chromatin remodeling and transcriptional regulations. The solution NMR structure of ARID3A ARID domain consists of eight alpha-helices alpha0-alpha7 and a short beta hairpin. Helix alpha0 and alpha1 form a V shape, helix alpha2-alpha4 and helix alpha5-alpha7 form two U shapes, and the V and two U shapes packed orthogonal to each other. The NMR structure of the ARID domain of human ARID3A reported here provides a structural basis for elucidating the regulatory mechanisms of ARID3A function, and the molecular mechanism of ARID3A interactions with DNA. It also has potential value in future drug discovery and design.
Solution NMR structure of the ARID domain of human AT-rich interactive domain-containing protein 3A: a human cancer protein interaction network target.,Liu G, Huang YJ, Xiao R, Wang D, Acton TB, Montelione GT Proteins. 2010 Jul;78(9):2170-5. doi: 10.1002/prot.22718. PMID:20455271[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R. A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence. Nat Cell Biol. 2002 Feb;4(2):148-53. PMID:11812999 doi:10.1038/ncb742
- ↑ Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA. E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53. Mol Cancer Res. 2003 Apr;1(6):438-44. PMID:12692263
- ↑ Liu G, Huang YJ, Xiao R, Wang D, Acton TB, Montelione GT. Solution NMR structure of the ARID domain of human AT-rich interactive domain-containing protein 3A: a human cancer protein interaction network target. Proteins. 2010 Jul;78(9):2170-5. PMID:20455271 doi:10.1002/prot.22718
