PX domain takes shape

In recent years, a number of protein domains have been identified that bind phosphoinositides and direct proteins to membrane targets. A recent addition to this group is the Phox homology or PX domain, a 120-amino acid domain conserved from yeast to humans, which is present in proteins involved in c...

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Bibliographic Details
Published inCurrent opinion in hematology Vol. 10; no. 1; p. 2
Main Authors Wientjes, Frans B, Segal, Anthony W
Format Journal Article
LanguageEnglish
Published United States 01.01.2003
Subjects
Animals
Binding Sites
Homeodomain Proteins - chemistry
Homeodomain Proteins - metabolism
Homeodomain Proteins - physiology
Humans
Phospholipids - metabolism
Protein Binding
Protein Structure, Tertiary
src Homology Domains
Substrate Specificity
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Summary:In recent years, a number of protein domains have been identified that bind phosphoinositides and direct proteins to membrane targets. A recent addition to this group is the Phox homology or PX domain, a 120-amino acid domain conserved from yeast to humans, which is present in proteins involved in cell signaling, protein sorting, vesicle fusion, and the assembly of components of the superoxide generating system of neutrophils. These domains have varying affinities for phosphatidylinositol-3-phosphate (PI(3)P), and PI(3,4) and (4,5) bisphosphates, which couple the PI kinase and phosphatase signaling networks to the assembly of proteins at membrane surfaces. These PX domains also contain a PXXP motif, allowing them to bind to proteins containing Src homology 3 (SH3) domains.
ISSN:1065-6251
DOI:10.1097/00062752-200301000-00002