The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes

Three-dimensional electron microscopy reconstructions of the human alpha(2)-macroglobulin (alpha(2)M) dimer and chymotrypsin-transformed alpha(2)M reveal the structural arrangement of the two dimers that comprise native and proteinase-transformed molecules. They consist of two side-by-side extended...

Ausführliche Beschreibung

Bibliographische Detailangaben

Veröffentlicht in:	The Journal of biological chemistry 2002-08, Vol.277 (31), p.28031-28037
Hauptverfasser:	Kolodziej, Steven J, Wagenknecht, Terence, Strickland, Dudley K, Stoops, James K
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha-Macroglobulins - chemistry alpha-Macroglobulins - ultrastructure Chymotrypsin - chemistry Chymotrypsin - ultrastructure Dimerization Humans Image Processing, Computer-Assisted Macromolecular Substances Microscopy, Electron Models, Molecular Protein Conformation Protein Subunits
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!