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1BC7

SERUM RESPONSE FACTOR ACCESSORY PROTEIN 1A (SAP-1)/DNA COMPLEX

Summary for 1BC7
Entry DOI10.2210/pdb1bc7/pdb
DescriptorDNA (5'-D(*GP*AP*CP*AP*GP*GP*AP*TP*GP*TP*G)-3'), DNA (5'-D(*CP*AP*CP*AP*TP*CP*CP*TP*GP*TP*C)-3'), PROTEIN (ETS-DOMAIN PROTEIN), ... (4 entities in total)
Functional Keywordsets domain, dna-binding domain, winged helix-turn-helix, dna-binding specificity, complex (dna-binding protein-dna), transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (human)
Cellular locationNucleus: P28324
Total number of polymer chains3
Total formula weight17926.61
Authors
Mo, Y.,Vaessen, B.,Johnston, K.,Marmorstein, R. (deposition date: 1998-05-05, release date: 1999-01-21, Last modification date: 2024-04-03)
Primary citationMo, Y.,Vaessen, B.,Johnston, K.,Marmorstein, R.
Structures of SAP-1 bound to DNA targets from the E74 and c-fos promoters: insights into DNA sequence discrimination by Ets proteins.
Mol.Cell, 2:201-212, 1998
Cited by
PubMed Abstract: SAP-1 is a member of the Ets transcription factors and cooperates with SRF protein to activate transcription of the c-fos protooncogene. The crystal structures of the conserved ETS domain of SAP-1 bound to DNA sequences from the E74 and c-fos promoters reveal that a set of conserved residues contact a GGA core DNA sequence. Discrimination for sequences outside this core is mediated by DNA contacts from conserved and nonconserved protein residues and sequence-dependent DNA structural properties characteristic of A-form DNA structure. Comparison with the related PU.1/DNA and GABPalpha/beta/DNA complexes provides general insights into DNA discrimination between Ets proteins. Modeling studies of a SAP-1/SRF/DNA complex suggest that SRF may modulate SAP-1 binding to DNA by interacting with its ETS domain.
PubMed: 9734357
DOI: 10.1016/S1097-2765(00)80130-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

226707

数据于2024-10-30公开中

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