Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide

Article Abstract:

The X-ray crystal structure of the tNS3 NS3 proteinase domain complexed with the NS3-binding region of NS4A is composed of two asymmetric units of tNS3:NS4A molecules. The complex exhibits a three dimensional structure that that adopts a chemotrypsin-like fold with two structural domains that is made of twisted and six-stranded beta sheets. Furthermore, the crystal structure of the complex is similar to the Sinbis virus core protein.

Author: Rice, C.M., Lin, C., Kim, J.L., Landro, J.A., Morgenstern, K.A., Fox, T., Dwyer, M.D., Chambers, S.P., Markland, W., Lepre, C.A., O'Malley, E.T., Harbenson, S.L., Murcko, M.A., Caron, P.R., Thomson, J.A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Analysis, Enzymes, Recombinant proteins, Enzyme structure-activity relationships

User Contributions:

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

CAPTCHA


Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein

Article Abstract:

Research was conducted to determine the crystal structure of the hexamerization domain of the N-ethylmaleimide-sensitive fusion protein, a cytosolic adenosine triphosphatase. At 1.75 A resolution, the structure was found to be composed of a nucleotide-binding and a helical domain. This structure exhibited similarities with the first two domains of the clamp-loading subunit of Escherichia coli's DNA polymerase III.

Author: Weis, William I., Whiteheart, Sidney W., Lenzen, Christian U., Steinmann, Diana
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Adenosine triphosphatase

User Contributions:

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

CAPTCHA


The structure of a Ca2+ -binding epidermal growth factor-like domain: its role in protein-protein interactions

Article Abstract:

The crystal structure of Ca2+ binding to epidermal growth factor-like (EGF-like) domains was determined at high resolution using human clotting factor IX complexed with Ca2+. Seven calcium ligands were identified indicating that Ca2+ binds to EGF-like domains, stabilizes the protein and mediates protein-protein interactions. EGF-like domains are common in many extracellular proteins.

Author: Brownlee, George G., Stuart, David, Rao, Zihe, Handford, Penny, Mayhew, Mark, Knott, Vroni
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
Calcium-binding proteins, Calcium binding proteins

User Contributions:

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

CAPTCHA


Subjects list: Proteins, Protein structure, Research
Similar abstracts:
  • Abstracts: Crystal structure of the Oxytricha nova Telomere end binding protein complexed with single strand DNA. The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering
  • Abstracts: Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Secretory phospholipase A2 generates the novel lipid mediator lysophosphatidic acid in membrane microvesicles shed from activated cells
  • Abstracts: Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein
  • Abstracts: E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells
  • Abstracts: Bc/10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types. Disruption of the architectural factor HMGI-C: DNA-binding AT hook motifs fused in lipomas to distinct transcriptional regulatory domains
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.