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2W73

High-resolution structure of the complex between calmodulin and a peptide from calcineurin A

Summary for 2W73
Entry DOI10.2210/pdb2w73/pdb
Related1AJI 1AUI 1CDL 1CLL 1IWQ 1J7O 1J7P 1K90 1K93 1LVC 1M63 1MF8 1NKF 1PK0 1S26 1SK6 1SW8 1WRZ 1XFU 1XFV 1XFW 1XFX 1XFY 1XFZ 1Y6W 1YRT 1YRU 1ZOT 2BE6 2F3Y 2F3Z 2JL2 2V01 2V02 2VAY
DescriptorCALMODULIN, SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM, CALCIUM ION, ... (4 entities in total)
Functional Keywordsmetal-binding protein, protein phosphatase, alternative splicing, phosphoprotein, ubl conjugation, calmodulin-binding, calcium, hydrolase, calmodulin, acetylation, methylation, polymorphism, metal-binding, zinc, iron, dimer, ef hand, nucleus, metal binding protein
Biological sourceHOMO SAPIENS
More
Cellular locationCell membrane : Q08209
Total number of polymer chains8
Total formula weight76069.54
Authors
Majava, V.,Kursula, P. (deposition date: 2008-12-19, release date: 2009-05-12, Last modification date: 2024-05-08)
Primary citationMajava, V.,Kursula, P.
Domain Swapping and Different Oligomeric States for the Complex between Calmodulin and the Calmodulin-Binding Domain of Calcineurin A
Plos One, 4:E5402-, 2009
Cited by
PubMed Abstract: Calmodulin (CaM) is a ubiquitously expressed calcium sensor that engages in regulatory interactions with a large number of cellular proteins. Previously, a unique mode of CaM target recognition has been observed in the crystal structure of a complex between CaM and the CaM-binding domain of calcineurin A.
PubMed: 19404396
DOI: 10.1371/JOURNAL.PONE.0005402
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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