Structure and function of the enigmatic Sec14 domain-containing proteins and theetiology of human disease-Reference-Cited by-同舟云学术

Structure and function of the enigmatic Sec14 domain-containing proteins and theetiology of human disease

Published:2008-08-01 Issue:4 Volume:3 Page:399-410
ISSN:1746-0875
Container-title:Future Lipidology
language:en
Short-container-title:Future Lipidology

Author:

Curwin Amy¹,McMaster Christopher¹

Affiliation:

1. Dalhousie UniversityDepartments of Pediatrics and Biochemistry & Molecular Biology, Atlantic Research Centre, Halifax, Nova Scotia B3H 4H7, Canada Tel.: ; Fax: ,

Publisher

Informa UK Limited

Subject

Biochemistry

Link

https://www.tandfonline.com/doi/pdf/10.2217/17460875.3.4.399

Reference101 articles.

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3. Schaaf G, Ortlund EA, Tyeryar KR et al.: Functional anatomy of phospholipid binding and regulation of phosphoinositide homeostasis by proteins of the sec14 superfamily. Mol. Cell 29, 191–206 (2008).

4. Crystal structure of phospholipid bound Sec14p and subsequent analysis demonstrates that phosphatidylcholine and phosphatidylinositol (PI) bind at distinct but overlapping sites and that function of Sec14p requires binding by both ligands in cis for Sec14p function.

5. Sha B, Phillips SE, Bankaitis VA, Luo M: Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. Nature 391, 506–510 (1998)

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