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

Curr Opin Struct Biol. 1999 Aug;9(4):428-32. doi: 10.1016/S0959-440X(99)80059-1.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

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
  • Phospholipases A / genetics
  • Phospholipases A / metabolism*
  • Phospholipids / metabolism
  • Protein Binding
  • Protein Conformation
  • Static Electricity
  • Swine
  • Tryptophan / physiology

Substances

  • Bee Venoms
  • Eicosanoids
  • Elapid Venoms
  • Liposomes
  • Membrane Lipids
  • Phospholipids
  • Tryptophan
  • Phospholipases A
  • Calcium