1aui

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spinqualitylabelsall models 1aui, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN CALCINEURIN HETERODIMER

Overview

Calcineurin (CaN) is a calcium- and calmodulin-dependent protein, serine/threonine phosphate which is critical for several important, cellular processes, including T-cell activation. CaN is the target of the, immunosuppressive drugs cyclosporin A and FK506, which inhibit CaN after, forming complexes with cytoplasmic binding proteins (cyclophilin and, FKBP12, respectively). We report here the crystal structures of, full-length human CaN at 2.1 A resolution and of the complex of human CaN, with FKBP12-FK506 at 3.5 A resolution. In the native CaN structure, an, auto-inhibitory element binds at the Zn/Fe-containing active site. The, metal-site geometry and active-site water structure suggest a catalytic, mechanism involving nucleophilic attack on the substrate phosphate by a, metal-activated ... [(full description)]

About this Structure

1AUI is a [Protein complex] structure of sequences from [Homo sapiens] with CA, ZN and FE as [ligands]. Active as [[1]], with EC number [3.1.3.16]. Full crystallographic information is available from [OCA].

Reference

Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex., Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al., Nature. 1995 Dec 7;378(6557):641-4. PMID:8524402

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