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4ZNX

Crystal structure of the Fyn-SH3 domain in complex with the high affinity peptide APP12

Summary for 4ZNX
Entry DOI10.2210/pdb4znx/pdb
Related3UA6 3UA7 4EIK
DescriptorTyrosine-protein kinase Fyn, APP12 (3 entities in total)
Functional Keywordsbeta shandwich, signaling protein
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm: P06241
Total number of polymer chains8
Total formula weight32039.45
Authors
Camara-Artigas, A. (deposition date: 2015-05-05, release date: 2016-06-29, Last modification date: 2024-01-10)
Primary citationCamara-Artigas, A.,Ortiz-Salmeron, E.,Andujar-Sanchez, M.,Bacarizo, J.,Martin-Garcia, J.M.
The role of water molecules in the binding of class I and II peptides to the SH3 domain of the Fyn tyrosine kinase.
Acta Crystallogr.,Sect.F, 72:707-712, 2016
Cited by
PubMed Abstract: Interactions of proline-rich motifs with SH3 domains are present in signal transduction and other important cell processes. Analysis of structural and thermodynamic data suggest a relevant role of water molecules in these protein-protein interactions. To determine whether or not the SH3 domain of the Fyn tyrosine kinase shows the same behaviour, the crystal structures of its complexes with two high-affinity synthetic peptides, VSL12 and APP12, which are class I and II peptides, respectively, have been solved. In the class I complexes two water molecules were found at the binding interface that were not present in the class II complexes. The structures suggest a role of these water molecules in facilitating conformational changes in the SH3 domain to allow the binding of the class I or II peptides. In the third binding pocket these changes modify the cation-π and salt-bridge interactions that determine the affinity of the binding. Comparison of the water molecules involved in the binding of the peptides with previous reported hydration spots suggests a different pattern for the SH3 domains of the Src tyrosine kinase family.
PubMed: 27599862
DOI: 10.1107/S2053230X16012310
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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