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2LCT

Solution structure of the Vav1 SH2 domain complexed with a Syk-derived doubly phosphorylated peptide

Summary for 2LCT
Entry DOI10.2210/pdb2lct/pdb
NMR InformationBMRB: 17632
DescriptorProto-oncogene vav, Tyrosine-protein kinase SYK (2 entities in total)
Functional Keywordsphosphopeptide, syk kinase, tyrosine kinase, protein-peptide complex, phosphorylated peptide, phosphotyrosine binding domain, b cell signaling protein, signaling protein
Biological sourceHomo sapiens (human)
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Cellular locationCell membrane (Probable): P48025
Total number of polymer chains2
Total formula weight14009.60
Authors
Chen, C.,Gorenstein, N.,Post, C. (deposition date: 2011-05-09, release date: 2011-06-01, Last modification date: 2023-06-14)
Primary citationChen, C.H.,Martin, V.A.,Gorenstein, N.M.,Geahlen, R.L.,Post, C.B.
Two closely spaced tyrosines regulate NFAT signaling in B cells via Syk association with Vav.
Mol.Cell.Biol., 31:2984-2996, 2011
Cited by
PubMed: 21606197
DOI: 10.1128/MCB.05043-11
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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