1HLO

THE CRYSTAL STRUCTURE OF AN INTACT HUMAN MAX-DNA COMPLEX: NEW INSIGHTS INTO MECHANISMS OF TRANSCRIPTIONAL CONTROL

Summary for 1HLO

• Entry DOI: 10.2210/pdb1hlo/pdb
• Descriptor: DNA (5'-D(*CP*AP*CP*CP*AP*CP*GP*TP*GP*GP*T)-3'), DNA (5'-D(*AP*CP*CP*AP*CP*GP*TP*GP*GP*TP*G)-3'), PROTEIN (TRANSCRIPTION FACTOR MAX), ... (4 entities in total)
• Functional Keywords: transcriptional regulation, dna binding, complex (transcription factor max-dna), transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P61244
• Total number of polymer chains: 4
• Total formula weight: 25793.35

Authors

Brownlie, P.,Ceska, T.A.,Lamers, M.,Romier, C.,Theo, H.,Suck, D. (deposition date: 1997-09-10, release date: 1997-10-27, Last modification date: 2024-02-07)

Primary citation

Brownlie, P.,Ceska, T.,Lamers, M.,Romier, C.,Stier, G.,Teo, H.,Suck, D.
The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control.
Structure, 5:509-520, 1997

PubMed Abstract: Max belongs to the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. Max is able to form homodimers and heterodimers with other members of this family, which include Mad, Mxi1 and Myc; Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement amongst these dimer forms provides a complex system of transcriptional regulation. Max is also regulated by phosphorylation at a site preceding the basic region. We report here the first crystal structure of an intact bHLHZ protein bound to its target site.

PubMed: 9115440
DOI: 10.1016/S0969-2126(97)00207-4

Experimental method

X-RAY DIFFRACTION (2.8 Å)