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1MSE

SOLUTION STRUCTURE OF A SPECIFIC DNA COMPLEX OF THE MYB DNA-BINDING DOMAIN WITH COOPERATIVE RECOGNITION HELICES

Summary for 1MSE
Entry DOI10.2210/pdb1mse/pdb
DescriptorDNA (5'-D(*CP*CP*TP*AP*AP*CP*TP*GP*AP*CP*AP*CP*AP*CP*AP*T)-3'), DNA (5'-D(*AP*TP*GP*TP*GP*TP*GP*TP*CP*AP*GP*TP*TP*AP*GP*G)-3'), C-Myb DNA-Binding Domain (3 entities in total)
Functional Keywordsdna, double helix, c-myb dna-binding domain, protooncogene product, dna binding protein-dna complex, dna binding protein/dna
Biological sourceMus musculus (house mouse)
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Cellular locationNucleus: P06876
Total number of polymer chains3
Total formula weight22472.17
Authors
Ogata, K.,Morikawa, S.,Nakamura, H.,Sekikawa, A.,Inoue, T.,Kanai, H.,Sarai, A.,Ishii, S.,Nishimura, Y. (deposition date: 1995-01-24, release date: 1995-03-31, Last modification date: 2024-05-22)
Primary citationOgata, K.,Morikawa, S.,Nakamura, H.,Sekikawa, A.,Inoue, T.,Kanai, H.,Sarai, A.,Ishii, S.,Nishimura, Y.
Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices.
Cell(Cambridge,Mass.), 79:639-648, 1994
Cited by
PubMed Abstract: The DNA-binding region of Myb consists of three imperfect tandem repeats (R1, R2, and R3). We have determined the solution structure of a specific DNA complex of the minimum DNA-binding domain (R2R3) by heteronuclear multidimensional NMR. Both R2 and R3 contain three helices, and the third helix in each is found to be a recognition helix. R2 and R3 are closely packed in the major groove, so that the two recognition helices contact each other directly to bind to the specific base sequence, AACNG cooperatively; this is a significant arrangement of recognition helices. The three key base pairs in this sequence are specifically recognized by Asn-183 (R3), Lys-182 (R3), and Lys-128 (R2). In contrast, R1 has no specific interactions with DNA from our NMR study of the DNA complex of the full DNA-binding domain (R1R2R3).
PubMed: 7954830
DOI: 10.1016/0092-8674(94)90549-5
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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