Chromosomal Protein, Nonhistone, HMG2
[HMGB2 contains two DNA-binding HMG-box domains (A and B) and a long acidic C-terminal domain. It binds DNA without sequence specificity, but has a high affinity for bent or distorted DNA, and bend linear DNA. The individual A and B boxes (which, although broadly similar, show both structural and functional differences) exhibit many of the structure-specific properties of the whole protein. The acidic tail modulates the affinity of the tandem HMG boxes in HMG2 for a variety of DNA targets, including four-way junctions, but not distorted DNA minicircles, to which the proteins bind with very high affinity. HMGB2 appears to play important architectural roles in the assembly of nucleoprotein complexes in a variety of biological processes, for example V(D)J recombination, the initiation of transcription, and DNA repair. (Biochem Soc Trans 2001 Aug;29(Pt 4):395-401) ( NCI )]
UMLS (NCI) C0019800- Amino Acid, Peptide, or Protein
- Biologically Active Substance
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