Structural insights into central hypertension regulation by human aminopeptidase A

Yang Yang; Chang Liu; Yi Lun Lin; Fang Li

doi:10.1074/jbc.M113.494955

Structural insights into central hypertension regulation by human aminopeptidase A

Yang Yang, Chang Liu, Yi Lun Lin, Fang Li

Pharmacology

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

34 Scopus citations

Abstract

Background:HumanaminopeptidaseA(APA) regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides. Results: We determined the crystal structures of APA complexed with different ligands and calcium. Conclusion: The S1 pocket of APA contains a calcium-binding site and accommodates only acidic residues. Significance: This study elucidates the calcium-modulated substrate specificity of APA and will aid in the development of antihypertensive APA inhibitors.

Original language	English (US)
Pages (from-to)	25638-25645
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	288
Issue number	35
DOIs	https://doi.org/10.1074/jbc.M113.494955
State	Published - Aug 30 2013

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title = "Structural insights into central hypertension regulation by human aminopeptidase A",

abstract = "Background:HumanaminopeptidaseA(APA) regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides. Results: We determined the crystal structures of APA complexed with different ligands and calcium. Conclusion: The S1 pocket of APA contains a calcium-binding site and accommodates only acidic residues. Significance: This study elucidates the calcium-modulated substrate specificity of APA and will aid in the development of antihypertensive APA inhibitors.",

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AU - Liu, Chang

AU - Lin, Yi Lun

AU - Li, Fang

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AB - Background:HumanaminopeptidaseA(APA) regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides. Results: We determined the crystal structures of APA complexed with different ligands and calcium. Conclusion: The S1 pocket of APA contains a calcium-binding site and accommodates only acidic residues. Significance: This study elucidates the calcium-modulated substrate specificity of APA and will aid in the development of antihypertensive APA inhibitors.

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Structural insights into central hypertension regulation by human aminopeptidase A

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