4LE9 : Crystal structure of a chimeric c-Src-SH3 domain

  • Emilia Ortiz-Salmeron (Contributor)
  • Sergio Martinez-Rodriguez (Contributor)
  • A. Cámara-Artigas (Contributor)
  • Jose M. Martin-Garcia (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2014-05-07
Deposition Date:2013-06-25
Revision Date:
Molecular Weight:8827.73
Macromolecule Type:Protein
Residue Count:78
Atom Site Count:483

In the Src Homology 3 domain (SH3) the RT and n-Src loops form a pocket that accounts for the specificity and affinity in binding of proline rich motifs (PRMs), while the distal and diverging turns play a key role in the folding of the protein. We have solved the structure of a chimeric mutant c-Src-SH3 domain where specific residues at the RT- and n-Src-loops have been replaced by those present in the corresponding Abl-SH3 domain. Crystals of the chimeric protein show a single molecule in the asymmetric unit, which appears in an unfolded-like structure that upon generation of the symmetry related molecules reveals the presence of a domain swapped dimer where both, RT- and n-Src loops, act as hinge loops. In contrast, the fold of the diverging type II β-turn and the distal loop are well conserved. Our results are the first evidence for the presence of a structured diverging type II β-turn in an unfolded-like intermediate of the c-Src-SH3 domain, which can be stabilized by interactions from the β-strands of the same polypeptide chain or from a neighboring one. Futhermore, this crystallographic structure opens a unique opportunity to study the effect of the amino acid sequence of the hinge loops on the 3D domain swapping process of c-Src-SH3.
Date made availableMay 7 2014

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