3MTT
Crystal structure of iSH2 domain of human p85beta, Northeast Structural Genomics Consortium Target HR5531C
Summary for 3MTT
| Entry DOI | 10.2210/pdb3mtt/pdb |
| Descriptor | Phosphatidylinositol 3-kinase regulatory subunit beta (2 entities in total) |
| Functional Keywords | pi3-kinase subunit p85-beta, inter-sh2 domain, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, signaling protein, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 22748.60 |
| Authors | Guan, R.,Schauder, C.,Ma, L.C.,Krug, R.M.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2010-04-30, release date: 2010-05-19, Last modification date: 2024-11-27) |
| Primary citation | Schauder, C.,Ma, L.C.,Krug, R.M.,Montelione, G.T.,Guan, R. Structure of the iSH2 domain of human phosphatidylinositol 3-kinase p85beta subunit reveals conformational plasticity in the interhelical turn region Acta Crystallogr.,Sect.F, 66:1567-1571, 2010 Cited by PubMed Abstract: Phosphatidylinositol 3-kinase (PI3K) proteins actively trigger signaling pathways leading to cell growth, proliferation and survival. These proteins have multiple isoforms and consist of a catalytic p110 subunit and a regulatory p85 subunit. The iSH2 domain of the p85β isoform has been implicated in the binding of nonstructural protein 1 (NS1) of influenza A viruses. Here, the crystal structure of human p85β iSH2 determined to 3.3 Å resolution is reported. The structure reveals that this domain mainly consists of a coiled-coil motif. Comparison with the published structure of the bovine p85β iSH2 domain bound to the influenza A virus nonstructural protein 1 indicates that little or no structural change occurs upon complex formation. By comparing this human p85β iSH2 structure with the bovine p85β iSH2 domain, which shares 99% sequence identity, and by comparing the multiple conformations observed within the asymmetric unit of the bovine iSH2 structure, it was found that this coiled-coil domain exhibits a certain degree of conformational variability or `plasticity' in the interhelical turn region. It is speculated that this plasticity of p85β iSH2 may play a role in regulating its functional and molecular-recognition properties. PubMed: 21139197DOI: 10.1107/S1744309110041333 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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