2LCS
Yeast Nbp2p SH3 domain in complex with a peptide from Ste20p
Summary for 2LCS
| Entry DOI | 10.2210/pdb2lcs/pdb |
| NMR Information | BMRB: 17629 |
| Descriptor | NAP1-binding protein 2, Serine/threonine-protein kinase STE20 (2 entities in total) |
| Functional Keywords | adaptor, transferase, signaling protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Cytoplasm: Q12163 Q03497 |
| Total number of polymer chains | 2 |
| Total formula weight | 10031.12 |
| Authors | Gorelik, M.,Davidson, A.R. (deposition date: 2011-05-07, release date: 2012-02-01, Last modification date: 2024-05-01) |
| Primary citation | Gorelik, M.,Davidson, A.R. Distinct Peptide Binding Specificities of Src Homology 3 (SH3) Protein Domains Can Be Determined by Modulation of Local Energetics across the Binding Interface. J.Biol.Chem., 287:9168-9177, 2012 Cited by PubMed Abstract: The yeast Nbp2p SH3 and Bem1p SH3b domains bind certain target peptides with similar high affinities, yet display vastly different affinities for other targets. To investigate this unusual behavior, we have solved the structure of the Nbp2p SH3-Ste20 peptide complex and compared it with the previously determined structure of the Bem1p SH3b bound to the same peptide. Although the Ste20 peptide interacts with both domains in a structurally similar manner, extensive in vitro studies with domain and peptide mutants revealed large variations in interaction strength across the binding interface of the two complexes. Whereas the Nbp2p SH3 made stronger contacts with the peptide core RXXPXXP motif, the Bem1p SH3b domain made stronger contacts with residues flanking the core motif. Remarkably, this modulation of local binding energetics can explain the distinct and highly nuanced binding specificities of these two domains. PubMed: 22277653DOI: 10.1074/jbc.M111.330753 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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