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TitleDynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its Activity.
Journal, issue, pagesStructure, Vol. 24, Page 1947-1959, Year 2016
Publish dateJun 20, 2014 (structure data deposition date)
AuthorsHuculeci, R. / Cilia, E. / Lyczek, A. / Buts, L. / Houben, K. / Seeliger, M.A. / van Nuland, N. / Lenaerts, T.
External linksStructure / PubMed:27692963
MethodsNMR (solution)
Structure data

PDB-2mqi:
human Fyn SH2 free state
Method: SOLUTION NMR

PDB-2mrj:
Structure of Fyn protein SH2 bound
Method: SOLUTION NMR

PDB-2mrk:
Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / SH2 domain / Fyn kinase / Src kinase / phosphorylated peptide

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