S100 protein-annexin interactions: a model of the (Anx2-p11)(2) heterotetramer complex

Citation
Jsd. Santos et al., S100 protein-annexin interactions: a model of the (Anx2-p11)(2) heterotetramer complex, BBA-MOL CEL, 1498(2-3), 2000, pp. 181-191
Citations number
24
Categorie Soggetti
Cell & Developmental Biology
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
ISSN journal
01674889 → ACNP
Volume
1498
Issue
2-3
Year of publication
2000
Pages
181 - 191
Database
ISI
SICI code
0167-4889(200012)1498:2-3<181:SPIAMO>2.0.ZU;2-S
Abstract
The (Anx2)(2)(p11)(2) heterotetramer has been implicated in endo- and exocy tosis in vivo and in liposome aggregation in vitro. Here we report on the m odelling of the heterotetramer complex using docking algorithms. Two types of models are generated-heterotetramer and heterooctamer. On the basis of t he agreement between the calculated (X-ray) electron density and the observ ed projected density from cryo-electron micrographs on the one hand, and ca lculated energy criteria on the other hand, the heterotetramer models are p roposed as the most probable, and one of them is selected as the best model . Analysis of this model at an atomic level suggests that the interaction b etween the Anx2 core and p11 has an electrostatic character, being stabilis ed primarily through charged residues. (C) 2000 Elsevier Science B.V. All r ights reserved.