Crystal structure of the human angiotensin-converting enzyme-lisinopril complex (Q24293072)

GOA release 2020-03-11

chloride ion binding

1 reference

GOA release 2020-03-11

author name string

Ramanathan Natesh

1

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Sylva L U Schwager

2

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Edward D Sturrock

3

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K Ravi Acharya

Structure of neurolysin reveals a deep channel that limits substrate access

4

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language of work or name

English

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publication date

30 January 2003

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published in

Nature

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volume

421

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issue

6922

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page(s)

551-4

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cites work

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Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus

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Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase

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Methods used in the structure determination of bovine mitochondrial F1 ATPase

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids

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Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning

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The critical role of tissue angiotensin-converting enzyme as revealed by gene targeting in mice

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Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme

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Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form

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Defining the boundaries of the testis angiotensin I-converting enzyme ectodomain.

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Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes

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Activation of angiotensin converting enzyme by monovalent anions

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Anion activation of angiotensin converting enzyme: dependence on nature of substrate

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Arg(1098) is critical for the chloride dependence of human angiotensin I-converting enzyme C-domain catalytic activity.

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Protein folds and families: sequence and structure alignments

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A new class of angiotensin-converting enzyme inhibitors

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A deeply recessed active site in angiotensin-converting enzyme is indicated from the binding characteristics of biotin-spacer-inhibitor reagents

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Functional residues at the active site of angiotensin converting enzyme

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Processing of X-ray diffraction data collected in oscillation mode

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Raster3D: photorealistic molecular graphics

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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