2jt4
From Proteopedia
Solution Structure of the Sla1 SH3-3-Ubiquitin Complex
Overview
The SH3 domain is a protein-protein interaction module commonly found in intracellular signaling and adaptor proteins. The SH3 domains of multiple endocytic proteins have been recently implicated in binding ubiquitin, which serves as a signal for diverse cellular processes including gene regulation, endosomal sorting, and protein destruction. Here we describe the solution NMR structure of ubiquitin in complex with an SH3 domain belonging to the yeast endocytic protein Sla1. The ubiquitin binding surface of the Sla1 SH3 domain overlaps substantially with the canonical binding surface for proline-rich ligands. Like many other ubiquitin-binding motifs, the SH3 domain engages the Ile44 hydrophobic patch of ubiquitin. A phenylalanine residue located at the heart of the ubiquitin-binding surface of the SH3 domain serves as a key specificity determinant. The structure of the SH3-ubiquitin complex explains how a subset of SH3 domains has acquired this non-traditional function.
About this Structure
2JT4 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis for ubiquitin recognition by SH3 domains., He Y, Hicke L, Radhakrishnan I, J Mol Biol. 2007 Oct 12;373(1):190-6. Epub 2007 Aug 17. PMID:17765920 Page seeded by OCA on Sun May 4 09:16:11 2008
Categories: Protein complex | Saccharomyces cerevisiae | He, Y. | Radhakrishnan, I. | Actin-binding | Cytoplasm | Cytoskeleton | Dna damage | Dna repair | Endocytosis | Monoubiquitin signaling | Nucleus | Phosphorylation | Sh3 | Sh3 domain | Signaling protein | Ubiquitin | Ubiquitin-binding motif | Ubl conjugation
