The PH superfold: a structural scaffold for multiple functions

Citation
N. Blomberg et al., The PH superfold: a structural scaffold for multiple functions, TRENDS BIOC, 24(11), 1999, pp. 441-445
Citations number
45
Categorie Soggetti
Biochemistry & Biophysics
Journal title
TRENDS IN BIOCHEMICAL SCIENCES
ISSN journal
09680004 → ACNP
Volume
24
Issue
11
Year of publication
1999
Pages
441 - 445
Database
ISI
SICI code
0968-0004(199911)24:11<441:TPSASS>2.0.ZU;2-R
Abstract
Pleckstrin homology (PH) domains form a structurally conserved family that is associated with many regulatory pathways within the cell. Domains with a nearly identical fold are found in other families that share no Sequence s imilarity, suggesting the existence of a stable PH superfold. The PH domain s generally function as regulated membrane-binding modules that bind to ino sitol lipids and respond to upstream signals by targeting the host proteins to the correct cellular sites. The other domains with a similar fold, such as the phosphotyrosine binding domains, recognize protein ligands.