The envelope glycoprotein from tick-borne encephalitis virus at 2 Angstrom resolution

Article Abstract:

A research study examined the crystallographically determined structure of a soluble fragment taken from the major envelope protein of a flavivirus. The analysis showed an unusual architecture in which the flat and elongated dimer extends toward a parallel direction to the viral membrane. The residues that affect monoclonal antibody binding are found on the protein's surface that faces outward. A possible receptor binding site may be inferred from the clustering of mutations that affect virulence in different flaviviruses. The clustering, mutational and biochemical data suggests a fusion-activating, conformational change scenario that results from a low hydrogen-ion concentration.

Analysis, Glycoproteins, Viral research, Virus research, Encephalitis, Viral, Viral encephalitis

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

Article Abstract:

The study of the crystal structure of the transcription factor NF-kappa-B p50 homodimer indicates that the Rel homology region folds into two different domains. The homodimer binds to the palindromic kappa-B site and the folded domains are identical to the domains found in the immunoglobulin superfamily. The undistorted B-DNA helix is covered by the p50 dimer, enabling specific contacts with the 10-base-pair kappa-B recognition site.

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

Article Abstract:

The Rel-homology region of the p50 subunit of the human transcription factor NF-kappa-B consists of two beta-barrel domains. The transcription factor binds itself as a homodimer to the DNA and the beta barrel domains grip the DNA in the primary grooves. A recognition loop which reacts with DNA bases is included in the amino-terminal specificity domain.

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