Sequence and structure of PCBP2 KH1-KH2. A, domain
structure of PCBP2. Similar domain structures are observed in other PCBPs.
B, sequence alignment of the KH1-KH2 domains from human PCBPs.
Secondary structures for PCBP2 KH1-KH2 were based on the NMR structure.
Residues that define the hydrophobic interfaces for KH1-KH2 interaction are
marked with * signs above the one-letter codes. The
conserved arginine residues involved in specific recognition of two
consecutive cytosine bases are marked with # signs. C, left: backbone
traces of the NMR ensemble of the 12 lowest-energy conformers of PCBP2
KH1-KH2. The orange ovals indicate the three less well-defined loop
regions: the variable loops within the KH1 and KH2 domains, and the linker
between the two domains. Middle and right, two different
views of a ribbon presentation of the lowest energy structure of PCBP2
KH1-KH2. The KH1 and KH2 domains are colored blue and red,
respectively, the linker is colored green. The secondary structural
elements are labeled.