Open AccessStructure of the SH3 domain of rat endophilin A2
Author(s) -
Loll Patrick J.,
Swain Evelyn,
Chen Yuan,
Turner Brian T.,
Zhang Jifang
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108007574
Subject(s) - sh3 domain , domain (mathematical analysis) , materials science , chemistry , proto oncogene tyrosine protein kinase src , receptor , mathematics , biochemistry , mathematical analysis
The crystal structure of the SH3 domain of rat endophilin A2 has been determined by the multiwavelength anomalous dispersion method and refined at a resolution of 1.70 Å to R and R free values of 0.196 and 0.217, respectively. The structure adheres to the canonical SH3‐domain fold and is highly similar to those of the corresponding domains of endophilins A1 and A3. An intermolecular packing interaction between two molecules in the lattice exploits features that are commonly observed in SH3‐domain ligand recognition, including the insertion of a proline side chain into the ligand‐binding groove of the protein and the recognition of a basic residue by a cluster of acidic side chains on the RT loop.