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Article

Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I.

Structure (London, England : 1993) - 1 Feb 2003

Clout Naomi J, Tisi Dominic, Hohenester Erhard

Abstract excerpt

Fasciclin I is an insect neural cell adhesion molecule consisting of four FAS1 domains, homologs of which are present in many bacterial, plant, and animal proteins. The crystal structure of FAS1 domains 3 and 4 of Drosophila fasciclin I reveals a novel domain fold, consisting of a seven-stranded beta wedge and a number of alpha helices. The two domains are arranged in a linear fashion and interact through a...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 12575939
DOI: 10.1016/s0969-2126(03)00002-9

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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