1H9O

PHOSPHATIDYLINOSITOL 3-KINASE, P85-ALPHA SUBUNIT: C-TERMINAL SH2 DOMAIN COMPLEXED WITH A TYR751 PHOSPHOPEPTIDE FROM THE PDGF RECEPTOR, CRYSTAL STRUCTURE AT 1.79 A

Summary for 1H9O

• Entry DOI: 10.2210/pdb1h9o/pdb
• Related: 1A0N 1AZG 1PBW 1PHT 1PIC 1PKS 1PKT
• Descriptor: PHOSPHATIDYLINOSITOL 3-KINASE, BETA-PLATELET-DERIVED GROWTH FACTOR RECEPTOR (3 entities in total)
• Functional Keywords: transferase/receptor, complex (phosphotransferase-receptor), phosphotransferase, sh2 domain, signal transduction, phosphoinositide 3-kinase, transferase-receptor complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: P09619
• Total number of polymer chains: 2
• Total formula weight: 13313.86

Authors

Pauptit, R.A.,Rowsell, S.,Breeze, A.L.,Murshudov, G.N.,Dennis, C.A.,Derbyshire, D.J.,Weston, S.A. (deposition date: 2001-03-14, release date: 2001-03-19, Last modification date: 2024-10-09)

Primary citation

Pauptit, R.A.,Dennis, C.A.,Derbyshire, D.J.,Breeze, A.L.,Weston, S.A.,Rowsell, S.,Murshudov, G.N.
NMR Trial Models: Experiences with the Colicin Immunity Protein Im7 and the P85Alpha C-Terminal Sh2-Peptide Complex
Acta Crystallogr.,Sect.D, 57:1397-, 2001

PubMed Abstract: Two cases of successful molecular replacement using NMR trial models are presented. One is the crystal structure of the Escherichia coli colicin immunity protein Im7; the other is a heretofore unreported crystal structure of a specific PDGF receptor-derived peptide complex of the carboxy-terminal SH2 domain from the p85alpha subunit of human phosphatidylinositol 3-OH kinase. In both cases, molecular replacement was non-trivial. Success was achieved using trial models that consisted of an ensemble of NMR structures from which the more flexible portions had been excised. Use of maximum-likelihood refinement proved critical to be able to refine the poor starting models. The challenges typical of the use of NMR trial models in molecular replacement are discussed.

PubMed: 11567151
DOI: 10.1107/S0907444901012434

Experimental method

X-RAY DIFFRACTION (1.79 Å)