Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction.

Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. Research Abstract Details 

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Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. Abstract Text:

Huiming Li,Lan Zhang,Anjana Rao,Stephen C Harrison,Patrick G Hogan,

The protein phosphatase calcineurin recognizes a wide assortment of substrates and controls diverse developmental and physiological pathways in eukaryotic cells. Dephosphorylation of the transcription factor NFAT and certain other calcineurin substrates depends on docking of calcineurin at a PxIxIT consensus site. We describe here the structural basis for recognition of the PxIxIT sequence by calcineurin. We demonstrate that the high-affinity peptide ligand PVIVIT adds as a beta-strand to the edge of a beta-sheet of calcineurin; that short peptide segments containing the PxIxIT consensus sequence suffice for calcineurin-substrate docking; and that sequence variations within the PxIxIT core modulate the K(d) of the interaction within the physiological range 1 microM to 1 mM. Calcineurin can adapt to a wide variety of substrates, because recognition requires only a PxIxIT sequence and because variation within the core PxIxIT sequence can fine-tune the affinity to match the physiological signalling requirements of individual substrates.

Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. Publishing Authors By Initials

H Li,L Zhang,A Rao,SC Harrison,PG Hogan,

For similar biological phenomena, cell phenomena, and immunity: cell physiology: cell communication: signal transduction research abstracts see: biological phenomena, cell phenomena, and immunity: cell physiology: cell communication: signal transduction research

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Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of molecular biology

VOLUME: 369

Page Numbers: 1296-306

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 19

MONTH: 04

YEAR: 2007

Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. Keywords Mesh Terms:

KEYWORDS: Signal Transduction

MESH TERMS: metabolism

Chemical & Substance for Abstract: Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. Information

Substance Name: Calcineurin

Registry Number: EC 3.1.3.-

Grant and Affiliation Information for Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction.

AFFILIATION: The CBR Institute, for Biomedical Research, 200 Longwood Avenue, Boston, MA 02115, USA.

Country: England

AGENCY: United States NIAID

GRANT: AI40127

ACRONYM: AI

MEDLINETA: J Mol Biol

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