hnRNP A1 Structure for Molecular Biology Show the: RBD1, only. RBD2, only. Whole protein. Rotate: X 90 X -90 Y 90 Y -90 Distances: Protein (length in units) Protein, (width in units) Reset
The two RNA-binding domains of hnRNP A1.
The human hnRNP A1 protein is involved in the packaging, splicing, and transport of mRNA. The two RNA-binding domains are shown using the Cartoon display. RBD1 (residues 1-87) is colored light blue; RBD2 (residues 105-180) is colored violet; and the linker segment between domains is blue. The N- and C-termini are labeled. (cf. Fig. 2 of Shamoo et al.).
Each domain has the RNP consensus sequence that is also found in more than 250 other protein sequences. This homologous sequence is proposed to fold into the conserved babbab fold seen here. (Color the structure by Group; click on the RBD1 button; and trace the chain from the blue N-terminus to the green C-terminus of domain 1. The same topology is seen in domain 2, colored from green to red.)
Highight the sidechains that are proposed to interact with RNA.
Those residues that are likely to interact nonspecifically (bases or backbone phosphates) are colored white. The residues that are likely to interact specifically (H-bonds to bases) are colored red. The latter group is labelled at their a-carbons.
Note the similar pattern of residues in each domain and the opposite polarity of each "RNA-binding platform". Zoom for a closer view of either RBD1 or RBD2. (cf. Table 3. of Shamoo et al.)
See the page on the homologous U1A structure for a display of the actual protein-RNA interactions found in that complex.
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Coordinates from 1HA1.pdb.