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PMID: 10449366 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Interfacial binding of secreted phospholipases A(2): more than electrostatics and a major role for tryptophan.

Current opinion in structural biology ·Vol. 9 ·No. 4 ·1999-08-00 ·Pages 428-32

Gelb MH, Cho W, Wilton DC

Abstract

Secreted phospholipases A(2) have similar catalytic sites, but vastly different interfacial binding surfaces that modulate their binding affinity for different kinds of phospholipid vesicles by several orders of magnitude. The structure/function principles that dictate both the differential interfacial binding and the physiological function of these enzymes are beginning to be unraveled.

MeSH Terms
Animals Bee Venoms/enzymology Binding Sites Calcium/physiology Catalysis Cattle Cell Membrane/metabolism Crystallography, X-Ray Eicosanoids/metabolism Elapid Venoms/enzymology Humans Liposomes/metabolism Membrane Lipids/metabolism Models, Molecular Mutagenesis, Site-Directed Phospholipases A/chemistry,genetics,metabolism Phospholipids/metabolism Protein Binding Protein Conformation Static Electricity Swine Tryptophan/physiology
Chemicals
Bee Venoms Eicosanoids Elapid Venoms Liposomes Membrane Lipids Phospholipids Tryptophan Phospholipases A Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gelb M H
Departments of Chemistry and Biochemistry, University of Washington, 351700, Seattle, WA 98195, USA. gelb@chem.washington.edu
Cho W
Wilton D C
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
1999-08-00
Pages
428-32
Language
English
Region
England
NLM ID
9107784
Subset
IM
Grants
NIGMS NIH HHS · GM52598 · United States
NIGMS NIH HHS · GM53987 · United States
NHLBI NIH HHS · HL36235 · United States
Wellcome Trust · United Kingdom
Corrections
CommentIn
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