Sandbox20: Difference between revisions
From Proteopedia
Jump to navigationJump to search
| Line 22: | Line 22: | ||
===The RTP Dimer=== | ===The RTP Dimer=== | ||
[[Image:RTP Dimerisation.jpg | thumb | upright=1.1| left| | [[Image:RTP Dimerisation.jpg | thumb | upright=1.1| left| Polar interactions between α4 helices facilitates RTP dimerisation.]] | ||
The structure of an RTP monomer bears greatest similarity to the "''classic winged-helix''" motif, in which 'wings' project from the loop between the final two β sheets of their compact αβααββ structure.<ref>PMID: 10679470</ref> The two major variations from this theme are the absence of a β1 sheet (the corresponding region is instead termed the β1 loop), and the presence of a fourth elongate α-helix at the C-terminus, which facilitates dimerisation. Each of these secondary structural elements are indicated in this <scene name='Sandbox20/2efw/8'>structure</scene>. | The structure of an RTP monomer bears greatest similarity to the "''classic winged-helix''" motif, in which 'wings' project from the loop between the final two β sheets of their compact αβααββ structure.<ref>PMID: 10679470</ref> The two major variations from this theme are the absence of a β1 sheet (the corresponding region is instead termed the β1 loop), and the presence of a fourth elongate α-helix at the C-terminus, which facilitates dimerisation. Each of these secondary structural elements are indicated in this <scene name='Sandbox20/2efw/8'>structure</scene>. | ||
