SUPERFAMILY 1.73 HMM library and genome assignments server

2phe B:61-126 PDB entry domain

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a+b) [ 53931] (334)
  Mainly antiparallel beta sheets (segregated alpha and beta regions)
Fold:   ssDNA-binding transcriptional regulator domain [ 54446]
  helix-swapped dimer of beta(4)-alpha motifs
Superfamily:   ssDNA-binding transcriptional regulator domain [ 54447] (4)
Family:   Transcriptional coactivator PC4 C-terminal domain [ 54448]
  dimer of two separate motifs
Protein:   Transcriptional coactivator PC4 C-terminal domain [54449]
   
PDB Entry Domain:   2phe B:61-126 [ 139693]


InterPro annotation
Cross references IPR009044 SSF54447 Protein matches
Abstract

This entry represents a ssDNA-binding transcriptional regulator domain consisting of a helix-swapped dimer of beta(4)-alpha motifs. This domain is found as a C-terminal domain in the transciptional co-activator PC4 (where it is a dimer of two separate motifs), and in the plant transciprional regulator PBF-2 (where it is a single chain domain formed by a tandem repeat of two motifs).

Transcriptional regulators play a critical role in controlling the level of transcription from specific genes in response to different stimuli. Members of this family of transcriptional regulators, which preferentially bind single-stranded DNA, include PBF-2 from plants, the mammalian nuclear factor 1-X (NF1-X), and positive cofactor 4 (PC4). These proteins are structurally similar, consisting of a helix-swapped dimer of beta(4)-alpha motifs.

The plant defence transcription factor PBF-2 is comprised of four p24 subunits that interact through a helix-loop-helix motif to produce a central pore [PubMed12080340]. PBF-2 functions as part of the plant¿s defence system in response to the detection of a pathogen. Upon stimulation, PBF-2 induces several signal transduction pathways leading to changes in the expression of defence genes, including the pathogenesis-related (PR) genes.

NF1-X is one of several NF1 proteins that function as transcription factors. NF1-X consists of two functionally distinct domains: a conserved N-terminal DNA-binding domain and a C-terminal transcriptional regulatory domain. NF1-X binds to the promoter for the 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase gene [PubMed10432316].

PC4 (or P15) possess the ability to co-activate and suppress transcription via its DNA-binding activity. PC4 has been shown to stimulate transcription in vitro with diverse activators, including VP16, thyroid hormone receptor, BRCA-1, often involving TFIIA. PC4 and TFIIA are thought to facilitate the assembly of the pre-initiation complex. The repressive activity of PC4 can be alleviated by the transcription factor TFIIH, which protects promoters from PC4 repression [PubMed12590132]. PC4 consists of two domains: an N-terminal regulatory domain and a C-terminal cryptic DNA-binding domain. The protein acts as a dimer with two ssDNA binding channels running in opposite directions to each other [PubMed9360603].


InterPro database

PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

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Internal database links

   
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Superfamily level

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