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Instruments / Technical Area	Publication Details	Published
B23-Circular Dichroism	The SH3 domain of HS1 protein recognizes lysine-rich polyproline motifs Guiliano Siligardi , Paolo Ruzza , Rohanah Hussain , Luca Cesaro , Anna Maria Brunati , Lorenzo A. Pinna , Arianna Donella-Deana Amino Acids 42 (4) DOI: 10.1007/s00726-011-0831-4 PMID: 21287358 Diamond Proposal Number(s): [2023] Show Abstract ▼ Abstract: HS1 is a protein involved in erythroid proliferation and apoptotic cell death, containing several structurally significant motifs including a C-terminal SH3 domain. HPK1 is a member of the Ste20-related kinase family, which contains four proline-rich sequences and is constitutively associated with HS1 in hematopoietic cells. Recombinant fusion protein GST-SH3HS1 was expressed to assess the binding properties of 16 peptides derived from the HPK1 proline-rich regions. The binding affinities were determined by non-immobilized ligand interaction assay by circular dichroism. Our results revealed that the classical PxxPxK class II binding motif is not sufficient to induce the interaction with the GST-SH3HS1 domain, an event dependent on the presence of additional basic residue(s) located at the C-terminus of the PxxPxK motif: Lys?5 in P2 peptide and Lys?8 in P4c peptide. Lys replacement by Arg residues decreases the ligand binding affinity. The finding that both SH3HS1 domain and full-length HS1 protein bind to P2 peptide with similar affinity demonstrates that the whole protein sequence does not affect the interaction properties of the domain. In silico models of SH3HS1 as a complex with P2 or P4c highlight the domain residues that interact with the recognition determinants of the peptide ligand and that cooperate in the complex stabilization.	Feb 2011
B23-Circular Dichroism	Recognition of lysine-rich peptideligands by murine cortactin SH3 domain: CD, ITC and NMR studies Chiara Rubini , Paolo Ruzza , Mark R. Spaller , D. Gomika Udugamasooriya , Massimo Ballanda , Steafno Mammi , Andrea Borgogno , Andrea Calderan , Luca Cesaro , Anna M. Brunati , Arianna Donella-Deana , Rohanah Hussain , Giuliano Siligardi Biopolymers DOI: 10.1002/bip.21350 Show Abstract ▼ Abstract: Cortactin is a ubiquitous actin-binding protein that regulates various aspects of cell dynamics and is implicated in the pathogenesis of human neoplasia. The sequence of cortactin contains a number of signaling motifs and an SH3 domain at the C-terminus, which mediates the interaction of the protein with several partners, including Shank2. A recombinant protein, comprising the murine cortactin SH3 domain fused to GST (GST-SH3(m-cort)), was prepared and used to assess the domain-binding affinity of potential peptide-ligands reproducing the proline-rich regions of human HPK1 and Shank2 proteins. The key residues involved in the SH3(m-cort) domain recognition were identified by three different approaches: non-immobilized ligand interaction assay by circular dichroism, isothermal titration calorimetry and nuclear magnetic resonance. Our results show that the classical PxxPxK class II binding motif is not sufficient to mediate the interaction with GST-SH3(m-cort), an event that depends on the presence of additional basic residues located at either the N- or the C-terminus of the PxxPxK motif Especially effective in promoting the peptide binding is a Lys residue at the -5 position, a determinant present in both P2 (HPK1 394403) and S1 (Shank2 1168-1189) peptides. GST-SH3(m-cort) exhibits the highest affinity toward peptide Si, which contains additional Lys residues at the -3, -5, and -7 positions, indicating that the optimal consensus motif may be KPPxPxKxKxK. These results are supported by the in silico models of SH3(m-cort) complexed with P2 or S1, which highlight the domain residues that interact with the recognition determinants of the peptide-ligand and cooperate in binding stabilization.	Nov 2009
	Effect of 4-fluoro-L-proline on the SH3 binding affinity Paolo Ruzza , Chiara Rubini , Andrea Calderan , Andrea Guiotto , Luca Cesaro , Anna M. Brunati , Arianna Donella-Deana , Rohanah Hussain , Giuliano Siligardi Peptides For Youth: The Proceedings Of The 20th American Peptide Symposium 611, 499-500 20th American Peptide Symposium DOI: 10.1007/978-0-387-73657-0_216 PMID: 19400283	Mar 2009

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