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6CPK

Solution structure of SH3 domain from Shank3

Summary for 6CPK
Entry DOI10.2210/pdb6cpk/pdb
NMR InformationBMRB: 30438
DescriptorSH3 and multiple ankyrin repeat domains protein 3 (1 entity in total)
Functional Keywordspsd, scaffold protein, postsynaptic density, protein binding
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight6616.58
Authors
Ishida, H.,Vogel, H.J. (deposition date: 2018-03-13, release date: 2018-08-15, Last modification date: 2024-05-01)
Primary citationIshida, H.,Skorobogatov, A.,Yamniuk, A.P.,Vogel, H.J.
Solution structures of the SH3 domains from Shank scaffold proteins and their interactions with Cav1.3 calcium channels.
FEBS Lett., 592:2786-2797, 2018
Cited by
PubMed Abstract: Shank proteins are abundant scaffold proteins in the postsynaptic density (PSD) region of brain synapses. Mutations in Shank proteins are associated with autism, schizophrenia, and Alzheimer's disease. To gain insights into Shank protein interactions at the PSD, we determined the solution structures of the src homology 3 (SH3) domains of all three mammalian Shank proteins. Our findings indicate that they have identical and typical SH3 folding motifs, but unusual target-binding pockets. An investigation into the interaction between the Shank SH3 domains and the proline-rich region of the Cav1.3 calcium channel revealed an atypical interaction in which the highly acidic specificity binding pocket of the SH3 domains binds to a Cav1.3 region containing a cluster of three Arg residues. Our study provides insights into Shank SH3-mediated interactions.
PubMed: 30058071
DOI: 10.1002/1873-3468.13209
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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