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Article

The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change.

The Journal of biological chemistry - 13 Apr 2007

Schelling Pierre, Guglielmi Kristen M, Kirchner Eva, Paetzold Bernhard, Dermody Terence S, Stehle Thilo

Abstract excerpt

Reovirus attachment protein sigma1 mediates engagement of receptors on the surface of target cells and undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway. The sigma1 protein is a filamentous, trimeric molecule with a globular beta-barrel head domain. An unusual cluster of aspartic acid residues sandwiched between hydrophobic tyrosines is located at the sigma1...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17303562
DOI: 10.1074/jbc.M610805200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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