3D1N

Structure of human Brn-5 transcription factor in complex with corticotrophin-releasing hormone gene promoter


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.51 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.212 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of human Brn-5 transcription factor in complex with CRH gene promoter.

Pereira, J.H.Kim, S.H.

(2009) J Struct Biol 167: 159-165

  • DOI: https://doi.org/10.1016/j.jsb.2009.05.003
  • Primary Citation of Related Structures:  
    3D1N

  • PubMed Abstract: 

    The Brn-5 protein, highly expressed in human brain, belongs to the POU family; a class of transcription factors involved in a wide variety of biological processes ranging from programming of embryonic stem cells to cellular housekeeping. This functional diversity is conferred by two DNA-binding subdomains that can assume several configurations due to a bipartite arrangement of POU-specific (POU(S)) and POU-homeo (POU(H)) subdomains separated by a linker region. The crystal structure of human Brn-5 transcription factor in complex with corticotrophin-releasing hormone (CRH) gene promoter reveals an unexpected recognition mode of the protein to its cognate DNA. Moreover, the structure also shows the role of the linker in allowing diverse configurations that can be assumed by the two subdomains.


  • Organizational Affiliation

    Department of Chemistry, University of California, Berkeley, CA 94720, USA.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
POU domain, class 6, transcription factor 1
I, J, K, L, M
I, J, K, L, M, N, O, P
151Homo sapiensMutation(s): 2 
Gene Names: POU6F1BRN5MPOUTCFB1
UniProt & NIH Common Fund Data Resources
Find proteins for Q14863 (Homo sapiens)
Explore Q14863 
Go to UniProtKB:  Q14863
PHAROS:  Q14863
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ14863
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
5'-D(*DAP*DGP*DCP*DAP*DTP*DAP*DAP*DAP*DTP*DAP*DAP*DTP*DAP*DA)-3'
A, C, E, G
14N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-D(*DTP*DTP*DAP*DTP*DTP*DAP*DTP*DTP*DTP*DAP*DTP*DGP*DCP*DT)-3'
B, D, F, H
14N/A
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
I, J, K, L, M
I, J, K, L, M, N, O, P
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.51 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.212 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 100.298α = 90
b = 112.06β = 90
c = 181.504γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
SOLVEphasing
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-05-26
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-10-20
    Changes: Database references, Derived calculations, Source and taxonomy, Structure summary