Literature summary for 2.7.1.137 extracted from

Batra-Safferling, R.; Granzin, J.; Moedder, S.; Hoffmann, S.; Willbold, D.
Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: role of the anchor residue in ligand binding (2009), Biol. Chem., 391, 33-42.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of GST-tagged PI3K SH3 domain in Escherichia coli strain Bl21	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified detagged recombinant PI3K SH3 domain, residues 1-83, crystallized in presence of peptide ligands PD1R or PD1, the crystals do not contain the PD1 ligand, instead, the ligand binding site is partially occupied by residues Arg18 and Trp55 from the symmetry-related PI3K SH3 molecule. Sitting drop vapor diffusion method by mixing of 0.001 ml of protein-peptide mixture and 0.001 ml of reservoir solution containing for PD1R crystals 100 mM CAPS buffer, pH 10.5, 2 M ammonium sulfate and 0.2 M lithium sulfate or for PD1 crystals 100 mM Na-citrate buffer, pH 5.5, 0.5 M ammonium sulfate and 1 M lithium sulfate, 17°C, several weeks, X-ray diffraction structure determination and analysis at 1.7 A resolution	Homo sapiens

Crystallization (Comment)

Organism

purified detagged recombinant PI3K SH3 domain, residues 1-83, crystallized in presence of peptide ligands PD1R or PD1, the crystals do not contain the PD1 ligand, instead, the ligand binding site is partially occupied by residues Arg18 and Trp55 from the symmetry-related PI3K SH3 molecule. Sitting drop vapor diffusion method by mixing of 0.001 ml of protein-peptide mixture and 0.001 ml of reservoir solution containing for PD1R crystals 100 mM CAPS buffer, pH 10.5, 2 M ammonium sulfate and 0.2 M lithium sulfate or for PD1 crystals 100 mM Na-citrate buffer, pH 5.5, 0.5 M ammonium sulfate and 1 M lithium sulfate, 17°C, several weeks, X-ray diffraction structure determination and analysis at 1.7 A resolution

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged PI3K SH3 domain from Escherichia coli strain BL21 by glutathione affinity chromatography, followed by removal of the tag and gel filtration	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	PI3K binds PD1 peptide, a 12-residue proline-rich peptide HSKRPLPPLPSL, and PD1R peptide, at the SH3 domain with type I ligand orientation of the bound peptide with an extended conformation where the central portion forms a left-handed type II polyproline, PPII, helix. The residue at anchor position P-3 is a tyrosine	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	PI3K contains a Src homology 3, SH3, domain, residues 1-83, overall structure, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
PI3K	-	Homo sapiens