2LCT
Solution structure of the Vav1 SH2 domain complexed with a Syk-derived doubly phosphorylated peptide
Summary for 2LCT
Entry DOI | 10.2210/pdb2lct/pdb |
NMR Information | BMRB: 17632 |
Descriptor | Proto-oncogene vav, Tyrosine-protein kinase SYK (2 entities in total) |
Functional Keywords | phosphopeptide, syk kinase, tyrosine kinase, protein-peptide complex, phosphorylated peptide, phosphotyrosine binding domain, b cell signaling protein, signaling protein |
Biological source | Homo sapiens (human) More |
Cellular location | Cell membrane (Probable): P48025 |
Total number of polymer chains | 2 |
Total formula weight | 14009.60 |
Authors | Chen, C.,Gorenstein, N.,Post, C. (deposition date: 2011-05-09, release date: 2011-06-01, Last modification date: 2023-06-14) |
Primary citation | Chen, 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: 21606197DOI: 10.1128/MCB.05043-11 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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