(Q27748097)

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The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits

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The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits (English)

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D B Huang

1

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T Huxford

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2

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Y Q Chen

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3

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G Ghosh

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4

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publication date

15 November 1997

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published in

Structure

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volume

5

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page(s)

1427-36

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issue

11

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cites work

Function and activation of NF-kappa B in the immune system

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The NF-kappa B and I kappa B proteins: new discoveries and insights

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https://api.crossref.org/works/10.1016%2FS0969-2126%2897%2900293-1

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Structure, regulation and function of NF-kappa B

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https://api.crossref.org/works/10.1016%2FS0969-2126%2897%2900293-1

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RelB, a new Rel family transcription activator that can interact with p50-NF-kappa B.

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Structure of NF-kappa B p50 homodimer bound to a kappa B site

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Structure of the NF-kappa B p50 homodimer bound to DNA

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Characterization of elements determining the dimerization properties of RelB and p50.

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AMoRe: an automated package for molecular replacement

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Accurate bond and angle parameters for X-ray protein structure refinement

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PROCHECK: a program to check the stereochemical quality of protein structures

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DOI

10.1016/S0969-2126(97)00293-1

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PubMed ID

9384558

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(Q27748097)

The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits

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