Parvin: Difference between revisions

When you <scene name='Alpha-parvin/Parvin/5'>align</scene> the structure of one of the <font color='DimGrey'>alpha-parvin-LD</font> complexes, say the one with LD1 peptide bound, and the structure of <font color='brown'>alpha-parvin on its own (apo)</font>, you also get a good overall overlap (disregarding the long loop between helices αC and αE which, as was said before, is relatively flexible), but you can see that the <scene name='Alpha-parvin/Parvin/6'>vicinity of the binding site</scene> has slightly altered conformation. In particular, the angle between the N-linker helix and αA widens by around 15° and the N-linker helix rotates.<ref>PMID: 18940607</ref> In this paragraph the binding of paxillin to the isolated C-terminal CH domain was described. However, the NMR measurements in solution confirmed that the rest of alpha-parvin molecule makes little energetic contribution to the binding. The pictue is not complete, though, since it is possible that the conformational alterations induced by LD binding in the N-terminal part of the C-terminal CH domain are somehow propagated to the nearby linker region and thus the rest of the molecule, possible affecting the behaviour of alpha-parvin towards other binding partners.

==References==

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