4GO6

Crystal structure of HCF-1 self-association sequence 1

Summary for 4GO6

• Entry DOI: 10.2210/pdb4go6/pdb
• Descriptor: HCF N-terminal chain 1, HCF C-terminal chain 1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: tandem fibronectin repeat, protein interaction, transcription, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P51610 P51610
• Total number of polymer chains: 4
• Total formula weight: 60678.86

Authors

Park, J.,Lammers, F.,Herr, W.,Song, J. (deposition date: 2012-08-18, release date: 2012-10-17, Last modification date: 2024-11-06)

Primary citation

Park, J.,Lammers, F.,Herr, W.,Song, J.
HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation
Proc.Natl.Acad.Sci.USA, 109:17430-17435, 2012

PubMed Abstract: Host-cell factor 1 (HCF-1) is an unusual transcriptional regulator that undergoes a process of proteolytic maturation to generate N- (HCF-1(N)) and C- (HCF-1(C)) terminal subunits noncovalently associated via self-association sequence elements. Here, we present the crystal structure of the self-association sequence 1 (SAS1) including the adjacent C-terminal HCF-1 nuclear localization signal (NLS). SAS1 elements from each of the HCF-1(N) and HCF-1(C) subunits form an interdigitated fibronectin type 3 (Fn3) tandem repeat structure. We show that the C-terminal NLS recruited by the interdigitated SAS1 structure is required for effective formation of a transcriptional regulatory complex: the herpes simplex virus VP16-induced complex. Thus, HCF-1(N)-HCF-1(C) association via an integrated Fn3 structure permits an NLS to facilitate formation of a transcriptional regulatory complex.

PubMed: 23045687
DOI: 10.1073/pnas.1208378109

Experimental method

X-RAY DIFFRACTION (2.7 Å)