Forkhead Box Protein 3: Difference between revisions
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Each domain-swapped dimer of FOXP3 makes extensive interactions with NFAT1 involving residues Thr359, Asn361, His365, Glu399 | Each domain-swapped dimer of FOXP3 makes extensive interactions with NFAT1 involving FOXP3 **hydrogen bonding residues** Thr359, Asn361, His365, while Glu399 and Glu401 of FOXP3 **interact with a string of basic residues** including Lys664, Arg665, Lys666, and Arg667., among others, which were critical in the [[FOXP2]]-NFAT1 interaction. These interactions allow FOXP3 and NFAT1 to bind more tightly together than other NFAT1 complexes formed with other Forkhead box proteins.<ref name="Chen"/> | ||
The FOXP3 Forkhead Domain forms a relatively unique **domain swapped dimer** that bridges two unique oligonucletodies. Here is a morph estimating the **transition from monomer to domain-swapped dimer**. | |||
<ref name="Chen"/> | <ref name="Chen"/> | ||
