High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target (Q24299744)

GOA release 2020-03-11

GDP binding

1 reference

GOA release 2020-03-11

author name string

Liqing Chen

1

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Enrico DiGiammarino

2

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Xiaoyin E Zhou

3

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Yujun Wang

4

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Diana Toh

5

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Thomas W Hodge

6

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Edward J Meehan

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

17 September 2004

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published in

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volume

279

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issue

38

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page(s)

40204-8

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High-resolution crystal structure of S. cerevisiae Ypt51(DeltaC15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis

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Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4.

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A novel Rab9 effector required for endosome-to-TGN transport

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Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for env incorporation into virions and infectivity

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The structural GDP/GTP cycle of Rab11 reveals a novel interface involved in the dynamics of recycling endosomes

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Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases

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High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop

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Structural plasticity of an invariant hydrophobic triad in the switch regions of Rab GTPases is a determinant of effector recognition

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inferred from DOI database lookup

7 January 2021

based on heuristic

Distinct structural elements of rab5 define its functional specificity.

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