1PKS: STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY

Citation:
Abstract
Src homology 3 (SH3) domains, which are found in many proteins involved in intracellular signal transduction, mediate specific protein-protein interactions. The three-dimensional structure of the SH3 domain in the p85 subunit of the phosphatidylinositol 3-kinase (PI3K) has been determined by multidimensional NMR methods. The molecule consists of four short helices, two beta turns, and two antiparallel beta sheets. The beta sheets are highly similar to corresponding regions in the SH3 domain of the tyrosine kinase Src, even though the sequence identity of the two domains is low. There is a unique 15 amino acid insert in PI3K that contains three short helices. There are substantial differences in the identity of the amino acids that make up the receptor site of SH3 domains. The results suggest that while the overall structures of the binding sites in the PI3K and Src SH3 domains are similar, their ligand binding properties may differ.
PDB ID: 1PKSDownload
MMDB ID: 50838
PDB Deposition Date: 1994/3/7
Updated in MMDB: 2017/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 1PKS: monomeric; determined by author
Molecular Components in 1PKS
Label Count Molecule
Protein (1 molecule)
1
Phosphatidylinositol 3-kinase P85-alpha Subunit SH3 Domain(Gene symbol: PIK3R1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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