1FU5: NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE COMPLEXED TO A DOUBLY PHOSPHORYLATED PEPTIDE DERIVED FROM POLYOMAVIRUS MIDDLE T ANTIGEN

Citation:
Abstract
The N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K) has a higher affinity for a peptide with two phosphotyrosines than for the same peptide with only one. This unexpected result was not observed for the C-terminal SH2 from the same protein. NMR structural analysis has been used to understand the behavior of the N-SH2. The structure of the free SH2 domain has been compared to that of the SH2 complexed with a doubly phosphorylated peptide derived from polyomavirus middle T antigen (MT). The structure of the free SH2 domain shows some differences from previous NMR and X-ray structures. In the N-SH2 complexed with a doubly phosphorylated peptide, a second site for phosphotyrosine interaction has been identified. Further, line shapes of NMR signals showed that the SH2 protein-ligand complex is subject to temperature-dependent conformational mobility. Conformational mobility is also supported by the spectra of the ligand peptide. A binding model which accounts for these results is developed.
PDB ID: 1FU5Download
MMDB ID: 162593
PDB Deposition Date: 2000/9/14
Updated in MMDB: 2018/05
Experimental Method:
solution nmr
Source Organism:
Rattus norvegicus
Similar Structures:
Molecular Components in 1FU5
Label Count Molecule
Proteins (2 molecules)
1
Phosphatidylinositol 3-kinase Regulatory Alpha Subunit(Gene symbol: Pik3r1)
Molecule annotation
1
Doubly Phosphorylated Middle T Antigen
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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