4LE9
Crystal structure of a chimeric c-Src-SH3 domain
Summary for 4LE9
| Entry DOI | 10.2210/pdb4le9/pdb |
| Related | 3FJ5 4JZ3 4JZ4 |
| Descriptor | Proto-oncogene tyrosine-protein kinase Src, TRIETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | beta shandwich, sh3, kinase, proly proline rich motifs, phosphorylation, transferase |
| Biological source | Gallus gallus (bantam,chickens) |
| Cellular location | Cell membrane (By similarity): P00523 |
| Total number of polymer chains | 1 |
| Total formula weight | 8827.73 |
| Authors | Camara-Artigas, A.,Martinez-Rodriguez, S.,Ortiz-Salmeron, E.,Martin-Garcia, J.M. (deposition date: 2013-06-25, release date: 2014-05-07, Last modification date: 2023-09-20) |
| Primary citation | Camara-Artigas, A.,Martinez-Rodriguez, S.,Ortiz-Salmeron, E.,Martin-Garcia, J.M. 3D domain swapping in a chimeric c-Src SH3 domain takes place through two hinge loops. J.Struct.Biol., 186:195-203, 2014 Cited by PubMed Abstract: 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have solved the structure of a chimeric mutant c-Src-SH3 domain where specific residues at the RT- and n-Src-loops have been replaced by those present in the corresponding Abl-SH3 domain.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. PubMed: 24556574DOI: 10.1016/j.jsb.2014.02.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.344 Å) |
Structure validation
Download full validation report
