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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title | Authors |
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19423 | Chemical Shifts: 2 sets |
Solution structure of the Vav1 SH2 domain complexed with a Syk-derived singly phosphorylated peptide |
Differential recognition of syk-binding sites by each of the two phosphotyrosine-binding pockets of the Vav SH2 domain.
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Carol Beth Post, Chih-Hong Chen, Dan Piraner, Nina M Gorenstein, Robert L Geahlen |
17632 | Chemical Shifts: 1 set |
Solution structure of the Vav1 SH2 domain complexed with a Syk-derived doubly phosphorylated peptide |
Two closely-spaced tyrosines regulate NFAT signaling in B cells via Syk association with Vav.
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Carol Beth Post, Chih-Hong Chen, Nina M Gorenstein, Robert L Geahlen, Victoria A Martin |