2f2p

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spinqualitylabelsall models 2f2p, resolution 2.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2F2P is a Single protein structure of sequence from Bos taurus with CA as ligand. Full crystallographic information is available from OCA.

Reference

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode., Ye Q, Li X, Wong A, Wei Q, Jia Z, Biochemistry. 2006 Jan 24;45(3):738-45. PMID:16411749

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