2fci Summary

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Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase

The structure was published by Groesch, T.D., Zhou, F., Mattila, S., Geahlen, R.L., and Post, C.B., in 2006 in a paper entitled "Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by syk tyrosine kinase" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2005.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Doubly phosphorylated peptide derived from Syk kinase comprising residues 338-350 and C-termainl SH2 domain from phospholipase C-gamma-1 comprising residues 663-759.

The molecule most likely forms heterodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
B Doubly phosphorylated peptide derived from Syk kinase comprising residues 338-350 Q32PK0 (314-326) (Q32PK0_BOVIN)search Bos taurussearch < 90% 14 100%
A C-termainl SH2 domain from phospholipase C-gamma-1 comprising residues 663-759 P08487 (663-759) (PLCG1_BOVIN)search Bos taurussearch < 90% 105 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q32PK0 (314 - 326) Doubly phosphorylated peptide derived from Syk kinase comprising residues 338-350
P08487 (663 - 759) C-termainl SH2 domain from phospholipase C-gamma-1 comprising residues 663-759 Bos taurus

Chain Structural classification (SCOP) Sequence family (Pfam)
B
A SH2 domainsearch SH2 domainsearch
Chain InterPro annotation
B
A SH2 domainsearch