Related Experiment Video
Updated: Jun 25, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
Published on: June 3, 2014
Structure of the trigonal crystal form of bovine annexin IV
G Zanotti1, G Malpeli, F Gliubich
1Department of Organic Chemistry, University of Padova, and Biopolymer Research Center, C.N.R., 35131 Padova, Italy.
Abstract:
The structure of a trigonal crystal form of N-terminally truncated [des-(1-9)] bovine annexin IV, an annexin variant that exhibits the distinctive property of binding both phospholipids and carbohydrates in a Ca2+-dependent manner, has been determined at 3 A (0.3 nm) resolution -space group: R3; cell parameters: a=b=118.560 (8) A and c=82.233 (6) A-. The overall structure of annexin IV, crystallized in the absence of Ca2+ ions, is highly homologous to that of the other known members of the annexin family. The trimeric assembly in the trigonal crystals of annexin IV is quite similar to that found previously in non-isomorphous crystals of human, chicken and rat annexin V and to the subunit arrangement in half of the hexamer of hydra annexin XII. Moreover, it resembles that found in two-dimensional crystals of human annexin V bound to phospholipid monolayers. The propensity of several annexins to generate similar trimeric arrays supports the hypothesis that trimeric complexes of such annexins, including annexin IV, may represent the functional units that interact with membranes.
More Related Videos
Related Concept Videos
Protein Organization
Protein Folding
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
ATP Synthase: Structure
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Type IV Collagen of Basal Lamina
A type IV collagen molecule has six alpha chains which can exist in...

