Abstracts - faqs.org

Abstracts

Zoology and wildlife conservation

Search abstracts:
Abstracts » Zoology and wildlife conservation

Structure of the UmuD' protein and its regulation in response to DNA damage

Article Abstract:

The crystal structure of the mutagenic protein UmuD of Escherichia coli at 2.5 angstrom resolution reveals globular heads folded in a rare beta-structure that cohere to form dimer molecules. The extended amino-acid tail congregate to form crystallized filaments. UmuD filament forms a scaffold on the RecA-DNA filament that places UmuC efficiently for interaction with DNA polymerase III holoenzyme. Analysis of the structure indicates that UmuD undergoes self-cleavage reactions during the global SOS response.

Author: Woodgate, Roger, McDonald, John P., Frank, Ekaterina G., Hendrickson, Wayne A., Levine, Arthur S., Peat, Thomas S.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Physiological aspects, DNA damage, Mutagens

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Structure of human follicle-stimulating hormone in complex with its receptor

Article Abstract:

The 2.9-angstrom-resolution structure of a partially deglycosylated complex of human follicle-stimulating hormone (FSH) bound to the extracellular hormone-binding domain of its receptor (FSHR(sub HB)) is presented. The analysis suggests that all glycoprotein hormones bind to their receptors in this mode and that binding specificity is mediated by key interaction sites both the common alpha- and hormone-specific beta-subunits

Author: Hendrickson, Wayne A., Qing R. Fan
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
United States, Science & research, Glycosylation, Structure, Follicle-stimulating hormone

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Structure of a C-type mannose-binding protein complexed with an oligosaccharide

Article Abstract:

The crystal structure of a calcium-dependent animal lectin, a type of mannose-binding carbohydrate recognition protein, shows the role of calcium ions in binding. The structure also sheds light on why these proteins bind some sugars and not others. For example, two oligosaccharide branches crosslink with the crystal to allow multivalent binding of one oligosaccharide chain.

Author: Weis, William I., Drickhamer, Kurt, Hendrickson, Wayne A.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Oligosaccharides, Lectins, Lectin structure-activity relationships

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research
Similar abstracts:
  • Abstracts: Structure of a cannabinoid receptor and functional expression of the cloned cDNA. Pain responses, anxiety and aggression in mice deficient in pre-proenkephalin
  • Abstracts: Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex
  • Abstracts: Structure of hisactophilin is similar to interleukin-1-beta and fibroblast growth factor. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
  • Abstracts: The buzz about pollination. Mystery of moribund marram. A leaf for all seasons
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.