Dimeric quaternary structure of human laforin

Rajeshwer S. Sankhala; Adem C. Koksal; Lan Ho; Felix Nitschke; Berge A. Minassian; Gino Cingolani

doi:10.1074/jbc.M114.627406

Dimeric quaternary structure of human laforin

Rajeshwer S. Sankhala, Adem C. Koksal, Lan Ho, Felix Nitschke, Berge A. Minassian, Gino Cingolani

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14 Scopus citations

Abstract

Background: Laforin is an essential glycogen phosphatase often mutated in Lafora disease. Results: Human laforin adopts a dimeric quaternary structure. Conclusion: Dimerization generates a unique active site crevice essential to recognize and dephosphorylate glycogen. Significance: We derived a complete structural model of human laforin using hybrid structural methods.

Original language	English (US)
Pages (from-to)	4552-4559
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	290
Issue number	8
DOIs	https://doi.org/10.1074/jbc.M114.627406
State	Published - Feb 20 2015

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M114.627406

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title = "Dimeric quaternary structure of human laforin",

abstract = "Background: Laforin is an essential glycogen phosphatase often mutated in Lafora disease. Results: Human laforin adopts a dimeric quaternary structure. Conclusion: Dimerization generates a unique active site crevice essential to recognize and dephosphorylate glycogen. Significance: We derived a complete structural model of human laforin using hybrid structural methods.",

author = "Sankhala, {Rajeshwer S.} and Koksal, {Adem C.} and Lan Ho and Felix Nitschke and Minassian, {Berge A.} and Gino Cingolani",

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AU - Sankhala, Rajeshwer S.

AU - Koksal, Adem C.

AU - Ho, Lan

AU - Nitschke, Felix

AU - Minassian, Berge A.

AU - Cingolani, Gino

PY - 2015/2/20

Y1 - 2015/2/20

N2 - Background: Laforin is an essential glycogen phosphatase often mutated in Lafora disease. Results: Human laforin adopts a dimeric quaternary structure. Conclusion: Dimerization generates a unique active site crevice essential to recognize and dephosphorylate glycogen. Significance: We derived a complete structural model of human laforin using hybrid structural methods.

AB - Background: Laforin is an essential glycogen phosphatase often mutated in Lafora disease. Results: Human laforin adopts a dimeric quaternary structure. Conclusion: Dimerization generates a unique active site crevice essential to recognize and dephosphorylate glycogen. Significance: We derived a complete structural model of human laforin using hybrid structural methods.

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Dimeric quaternary structure of human laforin

Abstract

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