The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3 |
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| Authors: | Salvador Casares Eiso AB Henk Eshuis Obdulio Lopez-Mayorga Nico AJ van Nuland Francisco Conejero-Lara |
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| Affiliation: | 1.Departamento de Química Física e Instituto de Biotecnología,Facultad de Ciencias, Universidad de Granada, Campus Fuentenueva s/n,Granada,Spain;2.Bijvoet Center, Department of NMR Spectroscopy,Utrecht University,Utrecht,The Netherlands |
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| Abstract: | Background SH3 domains are small protein modules of 60–85 amino acids that bind to short proline-rich sequences with moderate-to-low affinity and specificity. Interactions with SH3 domains play a crucial role in regulation of many cellular processes (some are related to cancer and AIDS) and have thus been interesting targets in drug design. The decapeptide APSYSPPPPP (p41) binds with relatively high affinity to the SH3 domain of the Abl tyrosine kinase (Abl-SH3), while it has a 100 times lower affinity for the α-spectrin SH3 domain (Spc-SH3). |
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