Sequence and structure of ENP and MEL4.
<p>A) AlphaFold-predicted structure for ENP [<a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1011217#pgen.1011217.ref027" target="_blank">27</a>,<a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1011217...
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2025
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| Summary: | <p>A) AlphaFold-predicted structure for ENP [<a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1011217#pgen.1011217.ref027" target="_blank">27</a>,<a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1011217#pgen.1011217.ref028" target="_blank">28</a>]. B) AlphaFold-predicted structure for MEL4/NPY4. Inset shows turn of the terminal region to highlight position of amino acid R450 (the analogue of R468 in ENP). Studied amino acid residues are indicated with arrows and position. Color code for the per residue confidence metrics in A and B) dark blue: pLDDT>90, light blue: 90 > pLDDT>70, yellow: 70 > pLDDT>50, orange pLDDT<50. C) Protein similarity schemes. The upper bar code compares MEL4 with ENP and the proteins MEL1-3; the lower ENP with MEL1-4; given are gray to black lines, indicating degree of similarity. Note the C-terminal region of ENP vs. the much shorter terminal region of MEL4. The inset depicts a similarity tree between these proteins based on Clustal comparison (<a href="https://www.ebi.ac.uk/jdispatcher/msa/clustalo" target="_blank">https://www.ebi.ac.uk/jdispatcher/msa/clustalo</a>). A schematic drawing indicates the regions tentatively separated by sequence similarity and AlphaFold-predicted structure.</p> |
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