Summary information and primary citation
- PDB-id
-
1zzj;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- structural protein-DNA
- Method
- X-ray (2.3 Å)
- Summary
- Structure of the third kh domain of hnrnp k in complex
with 15-mer ssDNA
- Reference
-
Backe PH, Messias AC, Ravelli RB, Sattler M, Cusack S
(2005): "X-Ray
Crystallographic and NMR Studies of the Third KH Domain
of hnRNP K in Complex with Single-Stranded Nucleic
Acids." STRUCTURE, 13,
1055-1067. doi: 10.1016/j.str.2005.04.008.
- Abstract
- The heterogeneous nuclear ribonucleoprotein (hnRNP) K
is implicated in multiple functions in the regulation of
gene expression and acts as a hub at the intersection of
signaling pathways and processes involving nucleic acids.
Central to its function is its ability to bind both ssDNA
and ssRNA via its KH (hnRNP K homology) domains. We
determined crystal structures of hnRNP K KH3 domain
complexed with 15-mer and 6-mer (CTC(4)) ssDNAs at 2.4 and
1.8 A resolution, respectively, and show that the KH3
domain binds specifically to both TCCC and CCCC sequences.
In parallel, we used NMR to compare the binding affinity
and mode of interaction of the KH3 domain with several
ssRNA ligands and CTC(4) ssDNA. Based on a structure
alignment of the KH3-CTC(4) complex with known structures
of other KH domains in complex with ssRNA, we discuss
recognition of tetranucleotide sequences by KH
domains.