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This review explores the up-and-down beta-barrel structures and the functional aspects of key viral proteins, including superoxide dismutase, plasma retinol-binding protein, neuraminidase, and hemagglutinin. We delve into the binding sites, structural motifs such as the Greek key, and the tetrameric subunit structures of influenza neuraminidase and hemagglutinin. The interactions at low pH and conformational changes related to fusion peptide functionality are highlighted. Key amino acid sequences are also discussed to illustrate their significance in structural biology.
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Distorted jerry roll structure of hemagglutinin globular head
Conformational change between high & low pH forms of hemagglutinin
Tamm Laboratory at http://faculty.virginia.edu/tamm/pages/project_fusion.html
Cell Vol 89, p263 (1997) Chan et al.Core Structure of gp41 from the HIV Envelope GlycoproteinThe envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a complex of gp120 and gp41. gp120 determines viral tropism by binding to target-cell receptors, while gp41 mediates fusion between viral and cellular membranes.