Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode

Summary for 2KDU
DescriptorCalmodulin, Protein unc-13 homolog A, CALCIUM ION (3 entities in total)
Functional Keywordsprotein, calmodulin, munc13, calcium, acetylation, methylation, alternative splicing, cell junction, cell membrane, coiled coil, cytoplasm, exocytosis, membrane, metal-binding, phorbol-ester binding, phosphoprotein, synapse, zinc, zinc-finger, metal binding protein-protein binding complex, metal binding protein-exocytosis complex, metal binding protein/exocytosis
Biological sourceXenopus laevis (clawed frog,common platanna,platanna)
Cellular locationCytoplasm: Q62768
Total number of polymer chains2
Total formula weight21058.49
Rodriguez-Castaneda, F.A.,Maestre-Martinez, M.,Coudevylle, N.,Dimova, K.,Jahn, O.,Junge, H.,Becker, S.,Brose, N.,Carlomagno, T.,Griesinger, C. (deposition date: 2009-01-19, release date: 2009-12-15, Last modification date: 2011-07-13)
Primary citationBecker, S.,Brose, N.,Carlomagno, T.,Coudevylle, N.,Dimova, K.,Griesinger, C.,Jahn, O.,Junge, H.,Lee, D.,Lipstein, N.,Maestre-Martinez, M.,Rodriguez-Castaneda, F.
Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity.
Embo J., 29:680-691, 2010
PubMed: 20010694
DOI: 110.1038/emboj.2009.373
PDB entries with the same primary citation
Experimental method
Structure validation
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PDB entries from 2021-06-09