Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid (Q27734262)

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S Yoo

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D K Worthylake

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M Houseweart

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C P Hill

Spontaneous mutations in the human immunodeficiency virus type 1 gag gene that affect viral replication in the presence of cyclosporins

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language of work or name

English

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publication date

27 December 1996

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published in

Cell

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volume

87

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page(s)

1285-94

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issue

7

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Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization.

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Functional domains of the capsid protein of human immunodeficiency virus type 1

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Structure of the amino-terminal core domain of the HIV-1 capsid protein

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Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes

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Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation

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Solution conformation of a cyclophilin-bound proline isomerase substrate

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Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy

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The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A

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Crystal structure of cyclophilin A complexed with substrate Ala-Pro suggests a solvent-assisted mechanism of cis-trans isomerization

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X-ray structure of a decameric cyclophilin-cyclosporin crystal complex

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Improved Fourier coefficients for maps using phases from partial structures with errors

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Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1101572

1101572

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference