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Article

Structure-function study of the N-terminal domain of exocyst subunit Sec3.

The Journal of biological chemistry - 2 Apr 2010

Baek Kyuwon, Knödler Andreas, Lee Sung Haeng, Zhang Xiaoyu, Orlando Kelly, Zhang Jian, Foskett Trevor J, Guo Wei, Dominguez Roberto

Abstract excerpt

The exocyst is an evolutionarily conserved octameric complex involved in polarized exocytosis from yeast to humans. The Sec3 subunit of the exocyst acts as a spatial landmark for exocytosis through its ability to bind phospholipids and small GTPases. The structure of the N-terminal domain of Sec3 (Sec3N) was determined ab initio and defines a new subclass of pleckstrin homology (PH) domains along with a new...

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Identifiers

PMID: 20139078
DOI: 10.1074/jbc.M109.096966
PMCID: PMC2856249

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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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