Three-dimensional structure of the Ras-interacting domain of RalGDS (Q27741370)

1

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10 November 2024

X. Weng

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10 November 2024

F. Hofer

3

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10 November 2024

G. S. Martin

4

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10 November 2024

S. H. Kim

5

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10 November 2024

publication date

August 1997

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language of work or name

English

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National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9253406

https://zenodo.org/record/1233566/files/article.pdf

10 November 2024

work available at URL

1 reference

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Nature structural biology

10 November 2024

published in

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volume

4

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issue

8

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page(s)

609-15

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cites work

Proteins regulating Ras and its relatives

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Mammalian Ras interacts directly with the serine/threonine kinase Raf

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The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue

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Evidence for a Ras/Ral signaling cascade

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Involvement of Ral GTPase in v-Src-induced phospholipase D activation

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The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain

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ralGDS family members interact with the effector loop of ras p21.

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A role for the Ral guanine nucleotide dissociation stimulator in mediating Ras-induced transformation

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A novel family of Ras-binding domains

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Crystal structure of a streptococcal protein G domain bound to an Fab fragment

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Complex formation between RAS and RAF and other protein kinases

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Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor

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Activation of Raf as a result of recruitment to the plasma membrane

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Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro

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Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator

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Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap

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Multiple Ras functions can contribute to mammalian cell transformation

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Determination of macromolecular structures from anomalous diffraction of synchrotron radiation

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Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface

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Structure of ubiquitin refined at 1.8 A resolution

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Quantitative structure-activity analysis correlating Ras/Raf interaction in vitro to Raf activation in vivo

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Ras/Rap effector specificity determined by charge reversal

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High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier

31 March 2020

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Improved methods for building protein models in electron density maps and the location of errors in these models

31 March 2020

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

31 March 2020

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Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins

31 March 2020

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Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution

31 March 2020

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inferred from DOI database lookup

7 January 2021

based on heuristic

Acta Crystallographica

29

D52

1033

Huang L.

1996

1 reference

10 November 2024

Identifiers

DOI

10.1038/NSB0897-609

0 references