BEN
Identifiers
SymbolBEN
PfamPF10523
InterProIPR018379
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the BEN domain is a protein domain which is found in diverse proteins including:

The BEN domain is predicted to function as an adaptor for the higher-order structuring of chromatin, and recruitment of chromatin modifying factors in transcriptional regulation. It has been suggested to mediate protein-DNA and protein-protein interactions during chromatin organization and transcription. The presence of BEN domains in a poxviral early virosomal protein and in polydnaviral proteins also suggests a possible role in the organisation of viral DNA during replication or transcription. They are generally linked to other globular domains with functions related to transcriptional regulation and chromatin structure, such as BTB, C4DM, and C2H2 fingers.[6]

This domain is predicted to form an all-alpha fold with four conserved helices. Its conservation pattern revealed several conserved residues, most of which have hydrophobic side-chains and are likely to stabilize the fold through helix-helix packing.[6] First human BEN domain (BEND3)structure is solved together with TPR (ERCC6L)domain and Stimulates the ERCC6L translocase and ATPase activities.[7]

References

  1. ^ Rampalli S, Pavithra L, Bhatt A, Kundu TK, Chattopadhyay S (October 2005). "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex". Molecular and Cellular Biology. 25 (19): 8415–29. doi:10.1128/MCB.25.19.8415-8429.2005. PMC 1265755. PMID 16166625.
  2. ^ Pavithra L, Rampalli S, Sinha S, Sreenath K, Pestell RG, Chattopadhyay S (2007). "Stabilization of SMAR1 mRNA by PGA2 involves a stem loop structure in the 5' UTR". Nucleic Acids Research. 35 (18): 6004–16. doi:10.1093/nar/gkm649. PMC 2094063. PMID 17726044.
  3. ^ Mackler S, Pacchioni A, Degnan R, Homan Y, Conti AC, Kalivas P, Blendy JA (February 2008). "Requirement for the POZ/BTB protein NAC1 in acute but not chronic psychomotor stimulant response". Behavioural Brain Research. 187 (1): 48–55. doi:10.1016/j.bbr.2007.08.036. PMC 2248375. PMID 17945361.
  4. ^ Krauss V, Dorn R (April 2004). "Evolution of the trans-splicing Drosophila locus mod(mdg4) in several species of Diptera and Lepidoptera". Gene. 331: 165–76. doi:10.1016/j.gene.2004.02.019. PMID 15094203.
  5. ^ Murcia-Nicolas A, Bolbach G, Blais JC, Beaud G (January 1999). "Identification by mass spectroscopy of three major early proteins associated with virosomes in vaccinia virus-infected cells". Virus Research. 59 (1): 1–12. doi:10.1016/S0168-1702(98)00114-2. PMID 10854161.
  6. ^ a b Abhiman S, Iyer LM, Aravind L (February 2008). "BEN: a novel domain in chromatin factors and DNA viral proteins". Bioinformatics. 24 (4): 458–61. doi:10.1093/bioinformatics/btn007. PMC 2477736. PMID 18203771.
  7. ^ Pitchai, Ganesha P.; Kaulich, Manuel; Bizard, Anna H.; Mesa, Pablo; Yao, Qi; Sarlos, Kata; Streicher, Werner W.; Nigg, Erich A.; Montoya, Guillermo; Hickson, Ian D. (2017-11-02). "A novel TPR–BEN domain interaction mediates PICH–BEND3 association". Nucleic Acids Research. 45 (19): 11413–11424. doi:10.1093/nar/gkx792. PMC 5737856.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR018379
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