Hi Tom, For acidic side-chains, these kind of interactions are described by Maria Flocco and Sherry Mowbray in: "Strange bedfellows: interactions between acidic side-chains in proteins." J. Mol. Biol. (1995) 254, 96-105.
Best regards, Martin On Mar 28, 2014, at 12:11 AM, Tom Peat <tom.p...@csiro.au> wrote: > Hello All, > > I am appealing to the community as I don't seem to be able to find through > Google what I am looking for, and I just don't have the ability to look > through every structure in the PDB to find this. > I have what I think is an interesting case: a two domain protein structure > with a mostly hydrophobic interface between the two domains- the kicker is > that I have two charged residues buried in this domain and they are > identical. > That is, I'm looking for an Arg-Arg or Asp-Asp type interaction (not Arg-Asp) > where these residues are less than 4 Angstroms apart. So I was wondering if > anyone had seen this in any other structure(s)? > The really interesting bit is that this interaction actually regulates the > activity of the enzyme domain although the domain interface isn't that close > to the catalytic site. > > Thanks in advance to all those who can find a reference to this kind of > interaction. > Cheers, tom
