Calbindin D28k and S100B have a similar interaction site with the lithium-inhibitable enzyme inositol monophosphatase-1: A new drug target site

Galila Agam; Orna Almog

doi:10.1021/jm5019324

Calbindin D28k and S100B have a similar interaction site with the lithium-inhibitable enzyme inositol monophosphatase-1: A new drug target site

Galila Agam
, Orna Almog

Department of Clinical Biochemistry and Pharmacology

Ben-Gurion University of the Negev

Research output: Contribution to journal › Article › peer-review

Abstract

Lithium salts (Li) are used to treat bipolar disorder patients. Li inhibits inositol-monophosphatase (IMPase)-1. Calbindin D28k (calbindin) and S100B enhance IMPase-1 activity. We compared our in silico model of the IMPase-1/calbindin complex with the crystal structure of S100B. Although calbindin and S100B have a low sequence homology, they seem to activate IMPase-1 in a similar mode. It is reasonable that molecules interfering with the interaction of IMPase-1 with either of its activators will have Li-like effects.

Original language	English
Pages (from-to)	2042-2044
Number of pages	3
Journal	Journal of Medicinal Chemistry
Volume	58
Issue number	4
DOIs	https://doi.org/10.1021/jm5019324
State	Published - 26 Feb 2015

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This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

ASJC Scopus subject areas

Molecular Medicine
Drug Discovery

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10.1021/jm5019324

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title = "Calbindin D28k and S100B have a similar interaction site with the lithium-inhibitable enzyme inositol monophosphatase-1: A new drug target site",

abstract = "Lithium salts (Li) are used to treat bipolar disorder patients. Li inhibits inositol-monophosphatase (IMPase)-1. Calbindin D28k (calbindin) and S100B enhance IMPase-1 activity. We compared our in silico model of the IMPase-1/calbindin complex with the crystal structure of S100B. Although calbindin and S100B have a low sequence homology, they seem to activate IMPase-1 in a similar mode. It is reasonable that molecules interfering with the interaction of IMPase-1 with either of its activators will have Li-like effects.",

author = "Galila Agam and Orna Almog",

note = "Publisher Copyright: {\textcopyright} 2015 American Chemical Society.",

year = "2015",

month = feb,

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doi = "10.1021/jm5019324",

language = "English",

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journal = "Journal of Medicinal Chemistry",

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T1 - Calbindin D28k and S100B have a similar interaction site with the lithium-inhibitable enzyme inositol monophosphatase-1

T2 - A new drug target site

AU - Agam, Galila

AU - Almog, Orna

PY - 2015/2/26

Y1 - 2015/2/26

N2 - Lithium salts (Li) are used to treat bipolar disorder patients. Li inhibits inositol-monophosphatase (IMPase)-1. Calbindin D28k (calbindin) and S100B enhance IMPase-1 activity. We compared our in silico model of the IMPase-1/calbindin complex with the crystal structure of S100B. Although calbindin and S100B have a low sequence homology, they seem to activate IMPase-1 in a similar mode. It is reasonable that molecules interfering with the interaction of IMPase-1 with either of its activators will have Li-like effects.

AB - Lithium salts (Li) are used to treat bipolar disorder patients. Li inhibits inositol-monophosphatase (IMPase)-1. Calbindin D28k (calbindin) and S100B enhance IMPase-1 activity. We compared our in silico model of the IMPase-1/calbindin complex with the crystal structure of S100B. Although calbindin and S100B have a low sequence homology, they seem to activate IMPase-1 in a similar mode. It is reasonable that molecules interfering with the interaction of IMPase-1 with either of its activators will have Li-like effects.

UR - https://www.scopus.com/pages/publications/84923899935

U2 - 10.1021/jm5019324

DO - 10.1021/jm5019324

M3 - Article

SN - 0022-2623

VL - 58

SP - 2042

EP - 2044

JO - Journal of Medicinal Chemistry

JF - Journal of Medicinal Chemistry

IS - 4

ER -

Calbindin D28k and S100B have a similar interaction site with the lithium-inhibitable enzyme inositol monophosphatase-1: A new drug target site

Abstract

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