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- W2045332582 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have solved the structure of a chimeric mutant c-Src-SH3 domain where specific residues at the RT- and n-Src-loops have been replaced by those present in the corresponding Abl-SH3 domain.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." @default.
- W2045332582 created "2016-06-24" @default.
- W2045332582 creator A5024054858 @default.
- W2045332582 creator A5025331331 @default.
- W2045332582 creator A5029435044 @default.
- W2045332582 creator A5090028669 @default.
- W2045332582 date "2014-04-01" @default.
- W2045332582 modified "2023-10-18" @default.
- W2045332582 title "3D domain swapping in a chimeric c-Src SH3 domain takes place through two hinge loops" @default.
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- W2045332582 doi "https://doi.org/10.1016/j.jsb.2014.02.007" @default.
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- W2045332582 hasPublicationYear "2014" @default.
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