FOXP2: Difference between revisions

&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;A very unique feature of the FOXP2-DNA structure is its ability to form a <scene name='FOXP2/Dimer_second/1'>domain swapped dimer</scene>. In the dimeric structure, two monomers exchange <scene name='FOXP2/Domain_swapped/1'>helix H3</scene>. The dimeric structure is stabilized by complex aromatic interactions involving <scene name='FOXP2/Aromatic/1'>aromatic residues</scene> 507, 509, 531, 534, 538, 540, 541, and 548. In typical FOX family proteins, dimerization is nearly impossible due to the presence of a proline at position 539, effectively preventing helix 2 and three from merging into a single long H3. In FOXP2, this proline is replaced with <scene name='FOXP2/Alanine/1'>an alanine</scene>, allowing the <scene name='FOXP2/Long_helices/1'>long helix</scene> to form. This feature is present in all FOXP proteins. Interestingly, the mutations Phe371Cys and Phe371Leu are known to cause FOXP dysfunction and speech issues, but <scene name='FOXP2/Buried_ph/1'>residue Phe 371 (Phe 538 here)</scene> is only involved in interactions in the FOXP2 dimeric form, highlighting the importance of the dimeric structure. The dimeric structure interacts with the DNA molecule to <scene name='FOXP2/Dimer_second_inter/1'>a far lesser extent</scene> than the monomeric form of FOXP2 however. A morph of the domain swapping can be <scene name='FOXP2/Domain_switching_morph/2'> seen here</scene>.<ref name="Chen"/>