2JT4

Solution Structure of the Sla1 SH3-3-Ubiquitin Complex

Summary for 2JT4

• Entry DOI: 10.2210/pdb2jt4/pdb
• Related: 1UBQ 1Z9Z
• Descriptor: Cytoskeleton assembly control protein SLA1, Ubiquitin (2 entities in total)
• Functional Keywords: endocytosis, monoubiquitin signaling, ubiquitin-binding motif, sh3, ubiquitin, actin-binding, cytoplasm, cytoskeleton, phosphorylation, sh3 domain, dna damage, dna repair, nucleus, ubl conjugation, signaling protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P32790
• Total number of polymer chains: 2
• Total formula weight: 16748.15

Authors

He, Y.,Radhakrishnan, I. (deposition date: 2007-07-18, release date: 2007-09-25, Last modification date: 2024-05-29)

Primary citation

He, Y.,Hicke, L.,Radhakrishnan, I.
Structural Basis for Ubiquitin Recognition by SH3 Domains
J.Mol.Biol., 373:190-196, 2007

PubMed Abstract: 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.

PubMed: 17765920
DOI: 10.1016/j.jmb.2007.07.074

Experimental method

SOLUTION NMR