2IUG

Crystal structure of the PI3-kinase p85 N-terminal SH2 domain

Summary for 2IUG

• Entry DOI: 10.2210/pdb2iug/pdb
• Related: 1A0N 1AZG 1H9O 1PBW 1PHT 1PIC 1PKS 1PKT 2IUH 2IUI
• Descriptor: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY ALPHA SUBUNIT (2 entities in total)
• Functional Keywords: transferase, polymorphism, ubl conjugation, phosphorylation, p85, sh2, pi3k, sh2 domain, sh3 domain, pi3-kinase, disease mutation
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 13939.57

Authors

Nolte, R.T.,Eck, M.J.,Schlessinger, J.,Shoelson, S.E.,Harrison, S.C. (deposition date: 2006-06-03, release date: 2006-06-06, Last modification date: 2024-05-08)

Primary citation

Nolte, R.T.,Eck, M.J.,Schlessinger, J.,Shoelson, S.E.,Harrison, S.C.
Crystal Structure of the Pi 3-Kinase P85 Amino-Terminal Sh2 Domain and its Phosphopeptide Complexes
Nat.Struct.Biol., 3:364-, 1996

PubMed Abstract: Crystal structures of the amino-terminal SH2 domain of the p85alpha subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that phosphopeptides bind in the two-pronged manner seen in high-affinity Lck and Src SH2 complexes, with conserved interactions between the domain and the peptide segment from phosphotyrosine to Met+3. Peptide binding requires the rearrangement of a tyrosyl side chain in the BG loop to create the hydrophobic Met+3 binding pocket. The structures suggest a mechanism for the biological specificity exhibited by PI 3-kinase in its interactions with phosphoprotein partners.

PubMed: 8599763
DOI: 10.1038/NSB0496-364

Experimental method

X-RAY DIFFRACTION (1.89 Å)