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1ZZK

Crystal Structure of the third KH domain of hnRNP K at 0.95A resolution

Summary for 1ZZK
Entry DOI10.2210/pdb1zzk/pdb
Related1ZZI 1ZZJ
DescriptorHeterogeneous nuclear ribonucleoprotein K (2 entities in total)
Functional Keywordskh domian, alpha-beta fold, dna binding protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P61978
Total number of polymer chains1
Total formula weight8910.09
Authors
Backe, P.H.,Messias, A.C.,Ravelli, R.B.,Sattler, M.,Cusack, S. (deposition date: 2005-06-14, release date: 2005-08-09, Last modification date: 2024-03-13)
Primary citationBacke, P.H.,Messias, A.C.,Ravelli, R.B.,Sattler, M.,Cusack, S.
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, 2005
Cited by
PubMed 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.
PubMed: 16004877
DOI: 10.1016/j.str.2005.04.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (0.95 Å)
Structure validation

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