1J5K

COMPLEX OF THE KH3 DOMAIN OF HNRNP K WITH A SINGLE_STRANDED 10MER DNA OLIGONUCLEOTIDE

Summary for 1J5K

• Entry DOI: 10.2210/pdb1j5k/pdb
• Descriptor: 5'-D(*AP*TP*AP*T*TP*CP*CP*CP*TP*C)-3', Heterogeneous nuclear ribonucleoprotein K (2 entities in total)
• Functional Keywords: single-stranded dna binding protein, transcription factor, hnrnp k, ct element, c-myc oncogene, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P61978
• Total number of polymer chains: 2
• Total formula weight: 12611.79

Authors

Clore, G.M.,Braddock, D.T. (deposition date: 2002-05-13, release date: 2002-07-10, Last modification date: 2023-12-27)

Primary citation

Braddock, D.T.,Baber, J.L.,Levens, D.,Clore, G.M.
Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA.
EMBO J., 21:3476-3485, 2002

PubMed Abstract: To elucidate the basis of sequence-specific single-stranded (ss) DNA recognition by K homology (KH) domains, we have solved the solution structure of a complex between the KH3 domain of the transcriptional regulator heterogeneous nuclear ribonucleoprotein K (hnRNP K) and a 10mer ssDNA. We show that hnRNP K KH3 specifically recognizes a tetrad of sequence 5'd-TCCC. The complex is stabilized by a dense network of methyl-oxygen hydrogen bonds involving the methyl groups of three isoleucine residues and the O2 and N3 atoms of the two central cytosine bases. Comparison with the recently solved structure of a specific protein-ssDNA complex involving the KH3 and KH4 domains of the far upstream element (FUSE) binding protein FBP suggests that the amino acid located five residues N-terminal of the invariant GXXG motif, which is characteristic of all KH domains, plays a crucial role in discrimination of the first two bases of the tetrad.

PubMed: 12093748
DOI: 10.1093/emboj/cdf352

Experimental method

SOLUTION NMR