Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

• HOME
• SETUP
• FAQ
• ABOUT
• GLOSSARY
• WHAT'S NEW
• FEEDBACK

BHD_1 Rad4 beta-hairpin domain 1

SMART accession number:	SM01030
Description:	This short domain is found in the Rad4 protein. This domain binds to DNA.
Interpro abstract (IPR018326):	This short domain is found in the Rad4 protein. This domain binds to DNA [ (PUBMED:17882165) ].
GO function:	DNA binding (GO:0003677)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 1657 BHD_1 domains in 1656 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing BHD_1 domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with BHD_1 domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing BHD_1 domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: chromatin
  Binding / catalysis: Binds to DNA

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Min JH, Pavletich NP
  • Recognition of DNA damage by the Rad4 nucleotide excision repair protein.
  • Nature. 2007; 449: 570-5
  • Display abstract

  • Mutations in the nucleotide excision repair (NER) pathway can cause thexeroderma pigmentosum skin cancer predisposition syndrome. NER lesions arelimited to one DNA strand, but otherwise they are chemically andstructurally diverse, being caused by a wide variety of genotoxicchemicals and ultraviolet radiation. The xeroderma pigmentosum C (XPC)protein has a central role in initiating global-genome NER by recognizingthe lesion and recruiting downstream factors. Here we present the crystalstructure of the yeast XPC orthologue Rad4 bound to DNA containing acyclobutane pyrimidine dimer (CPD) lesion. The structure shows that Rad4inserts a beta-hairpin through the DNA duplex, causing the two damagedbase pairs to flip out of the double helix. The expelled nucleotides ofthe undamaged strand are recognized by Rad4, whereas the two CPD-linkednucleotides become disordered. These findings indicate that the lesionsrecognized by Rad4/XPC thermodynamically destabilize the Watson-Crickdouble helix in a manner that facilitates the flipping-out of two basepairs.

• Structure (3D structures containing this domain)

• 3D Structures of BHD_1 domains in PDB

  PDB code	Main view	Title
  2qsf		Crystal structure of the Rad4-Rad23 complex
  2qsg		Crystal structure of Rad4-Rad23 bound to a UV-damaged DNA
  2qsh		Crystal structure of Rad4-Rad23 bound to a mismatch DNA
  4yir		4YIR

• Links (links to other resources describing this domain)

• INTERPRO	IPR018326
  PFAM	BHD_1

Send comments to Ivica Letunic