| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophysical Journal 67: 493-504 (1994)
© 1994 the Biophysical Society
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticutt 06511.
ABSTRACT
Biochemical and structural data suggest that electrostatic forces play a critical role in the binding of secretory phospholipases A2 to substrate aggregates (micelles, vesicles, monolayers, and membranes). This initial binding (adsorption) of the enzyme to the interface is kinetically distinct from the subsequent binding of substrate to the buried active site. Thus, in the absence of specific active-site interactions, electrostatic forces operating at the molecular surface may orient and hold the enzyme at the interface. We have calculated the electrostatic potentials for 10 species of secretory phospholipases A2 whose atomic coordinates have been determined by x-ray crystallography. Most of these enzymes show a marked electrostatic sidedness that is accentuated to a variable degree by the presence of the essential cofactor calcium ion. This asymmetry suggests a discrete interfacial binding region on the protein's surface, the location of which is in general agreement with proposals derived from the results of chemical modification, mutational, and crystallographic experiments.
This article has been cited by other articles:
 |
|
 |
|
  C. N. Birts, C. H. Barton, and D. C. Wilton A Catalytically Independent Physiological Function for Human Acute Phase Protein Group IIA Phospholipase A2: CELLULAR UPTAKE FACILITATES CELL DEBRIS REMOVAL J. Biol. Chem., February 22, 2008; 283(8): 5034 - 5045. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Linderoth, T. L. Andresen, K. Jorgensen, R. Madsen, and G. H. Peters Molecular Basis of Phospholipase A2 Activity toward Phospholipids with sn-1 Substitutions Biophys. J., January 1, 2008; 94(1): 14 - 26. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O Cremona and P De Camilli Phosphoinositides in membrane traffic at the synapse J. Cell Sci., January 3, 2001; 114(6): 1041 - 1052. [Abstract] [PDF]
|
|
|
|
|
|
S. K. Han, E. T. Yoon, D. L. Scott, P. B. Sigler, and W. Cho Structural Aspects of Interfacial Adsorption. A CRYSTALLOGRAPHIC AND SITE-DIRECTED MUTAGENESIS STUDY OF THE PHOSPHOLIPASE A2 FROM THE VENOM OF AGKISTRODON PISCIVORUS PISCIVORUS J. Biol. Chem., February 7, 1997; 272(6): 3573 - 3582. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Soubeyrand, A. Khadir, Y. Brindle, and P. Manjunath Purification of a Novel Phospholipase A2 from Bovine Seminal Plasma J. Biol. Chem., January 3, 1997; 272(1): 222 - 227. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B Honig and A Nicholls Classical electrostatics in biology and chemistry Science, May 26, 1995; 268(5214): 1144 - 1149. [Abstract] [PDF]
|
|
|
|
|
|
R. Dua, S.-K. Wu, and W. Cho A Structure-Function Study of Bovine Pancreatic Phospholipase A(2) Using Polymerized Mixed Liposomes J. Biol. Chem., January 6, 1995; 270(1): 263 - 268. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. M. Harris, S. K. Smith, and J. D. Bell Physical Properties of Erythrocyte Ghosts That Determine Susceptibility to Secretory Phospholipase A2 J. Biol. Chem., June 15, 2001; 276(25): 22722 - 22731. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. A. Beers, A. G. Buckland, R. S. Koduri, W. Cho, M. H. Gelb, and D. C. Wilton The Antibacterial Properties of Secreted Phospholipases A2. A MAJOR PHYSIOLOGICAL ROLE FOR THE GROUP IIA ENZYME THAT DEPENDS ON THE VERY HIGH pI OF THE ENZYME TO ALLOW PENETRATION OF THE BACTERIAL CELL WALL J. Biol. Chem., January 11, 2002; 277(3): 1788 - 1793. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
