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Structure paper

TitleStructure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins.
Journal, issue, pagesSci Adv, Vol. 4, Page eaau4130-eaau4130, Year 2018
Publish dateOct 19, 2017 (structure data deposition date)
AuthorsJemth, P. / Karlsson, E. / Vogeli, B. / Guzovsky, B. / Andersson, E. / Hultqvist, G. / Dogan, J. / Guntert, P. / Riek, R. / Chi, C.N.
External linksSci Adv / PubMed:30397651
MethodsNMR (solution)
Structure data

PDB-6es5:
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins
Method: SOLUTION NMR

PDB-6es6:
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins
Method: SOLUTION NMR

PDB-6es7:
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / NCBD / CID / Complex / IDP

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