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Article

Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily.

Protein science : a publication of the Protein Society - 1 Sept 2008

Ohnishi Satoshi, Tochio Naoya, Tomizawa Tadashi, Akasaka Ryogo, Harada Takushi, Seki Eiko, Sato Manami, Watanabe Satoru, Fujikura Yukiko, Koshiba Seizo, Terada Takaho, Shirouzu Mikako, Tanaka Akiko, Kigawa Takanori, Yokoyama Shigeyuki

Abstract excerpt

The second WW domain in mammalian Salvador protein (SAV1 WW2) is quite atypical, as it forms a beta-clam-like homodimer. The second WW domain in human MAGI1 (membrane associated guanylate kinase, WW and PDZ domain containing 1) (MAGI1 WW2) shares high sequence similarity with SAV1 WW2, suggesting comparable dimerization. However, an analytical ultracentrifugation study revealed that MAGI1 WW2 (Leu355-Pro390)...

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Share to Cell Adhesion Molecules
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 18562638
DOI: 10.1110/ps.035329.108
PMCID: PMC2525516

Genes

MAGI1
SAV1

Provenance

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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