2F2O

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

Summary for 2F2O

• Entry DOI: 10.2210/pdb2f2o/pdb
• Related: 2f2p
• Descriptor: Calmodulin fused with calmodulin-binding domain of calcineurin, CALCIUM ION (3 entities in total)
• Functional Keywords: ef-hands, calcium, calmodulin, calcineurin, metal binding protein
• Biological source: Bos taurus (cattle); More
• Total number of polymer chains: 2
• Total formula weight: 40171.13

Authors

Ye, Q.,Wong, A.,Jia, Z. (deposition date: 2005-11-17, release date: 2006-02-21, Last modification date: 2023-08-23)

Primary citation

Ye, Q.,Li, X.,Wong, A.,Wei, Q.,Jia, Z.
Structure of calmodulin bound to a calcineurin Peptide: a new way of making an old binding mode.
Biochemistry, 45:738-745, 2006

PubMed Abstract: Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.

PubMed: 16411749
DOI: 10.1021/bi0521801

Experimental method

X-RAY DIFFRACTION (2.17 Å)