Chapter category: Cell Metabolism
Annexin 1 Crystal Structure: Interaction of Annexins with Membranes
Annexins: Biological Importance and Annexin-Related Pathologies
Edited by: Joanna Bandorowicz-PikulaISBN: 0-306-47834-X
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Chapter authors:
Anja Rosengarth and Hartmut Luecke
Annexins are structurally divided into a highly conserved core domain and a variable N-terminal domain. The core domain mediates the calcium-dependent phospholipid binding of annexins, whereas the N-terminal domain, which is unique in sequence and length for each member of this protein family, is responsible for the specificity among the different members. Annexin 1 has been shown to possess membrane aggregation and fusion activity in the presence of calcium in vitro. Due to the high sequence homology of the core domain among different annexins, the property of membrane aggregation has been attributed to the N-terminal domain. For instance, a chimera protein comprising the core of annexin 5, which by itself does not exhibit membrane aggregation properties, and the N-terminal domain of annexin 1 is able to induce membrane aggregation. Numerous three-dimensional structures of annexins have been solved using x-ray crystallography, however, none reveal the tertiary structure of an N-terminal domain or its interaction with the core domain. We have solved the x-ray structure of full-length annexin 1 with an N-terminal domain comprising 42 amino acids in the absence of calcium ions at 1.8 Å resolution. Residues 2-26 of the N-terminal domain exhibit a mainly a-helical conformation with a kink at residue 17. Helix NA (residues 2 to 16) inserts into repeat III of the core domain thereby replacing the old helix D. Helix D on the other hand unfolds into an extended loop that forms a flap over the top of helix NA of the N-terminal domain. As a result, the type II calcium-binding site located in core repeat III is destroyed because the “capping residue” for calcium ion coordination is not in the proper conformation/location any more. Also presented in this article is the structure of full-length annexin 1 in the presence of 1 mM CaCl2. The structure of full-length annexin 1 in the absence of calcium ions is thought to represent the “inactive” form of the protein. We provide a model for the annexin 1-induced membrane aggregation and discuss it in light of the literature published to date.
Additional chapters from this book:
Annexin II: Analysis of a Pleiotropic Protein
Nolan R. Filipenko and David M. Waisman
The annexins are classically characterized as a family of proteins capable of binding to acidic phospholipids in a Ca2+-dependent manner. The interaction of these proteins with the plasma membra...
Annexin 1 Crystal Structure: Interaction of Annexins with Membranes
Anja Rosengarth and Hartmut Luecke
Annexins are structurally divided into a highly conserved core domain and a variable N-terminal domain. The core domain mediates the calcium-dependent phospholipid binding of annexins, whereas t...
Role of Annexin II Tetramer in the Regulation of Plasmin Activity
Kyu-Sil Choi, Darin K. Fogg, Sandra L. Fitzpatrick and David M. Waisman
The zymogen plasminogen is present in the plasma at a concentration of 2 mM and is converted to enzymatically active plasmin by plasminogen activators (PAs) such as tissue-type PA (tPA) or uroki...
Structure, Function and Evolution of the Annexin Gene Superfamily
Maria Pilar Fernandez and Reginald O. Morgan
The annexin gene superfamily features a unique, conserved structure of 4 homologous repeats with affinity for calcium, phospholipids and indeterminate receptors involved in calcium metabolism, c...
Self-Assembly of Annexin A5 on Lipid Membranes
Natalia Govorukhina, Wilma Bergsma-Schutter, Christine Mazères-Dubut, Serge Mazères, Eugenia Drakopoulou, Leonid Bystrykh, Frank Oling, Anneke Mukhopadhyay, Ilya Reviakine, Joséphine Lai Kee Him and Alain Brisson
This Chapter focuses on the property exhibited by several annexins to self-assemble as two-dimensional (2D) ordered arrays on membrane surfaces, a property that may be responsible for (some of...
Annexinopathy in the Antiphospholipid Syndrome
Jacob H. Rand and Xiao-Xuan Wu
The antiphospholipid (aPL) antibody syndrome is perhaps among the first annexinopathies identified. This Chapter will describe the syndrome and review the role of annexin V in its pathophysiol...
Acidic pH-Induced Ion Channels Formed by Annexin A6: Transformation of the Molecule from Soluble to Membrane Integral Protein
Slawomir Pikula
It has been recently described that annexin A6 (ANXA6), a member of the annexin family of human and verterbrate homologous Ca2+- and lipid-binding proteins, interacts with membra...
Annexin Gene Knock-Out Models
Alejandra Tomas, Matthew J. Hayes, Debipriya Das, Barry P. Young and Stephen E. Moss
Progress in understanding the functions of annexins has accelerated recently through the generation of cell lines and mice containing targeted disruptions of annexin genes. Annexin null mutant...
Annexin V: Stimulation-Dependent Association with Membrane Proteins
Eleni Tzima and John H. Walker
Annexin V relocates to specific cellular membranes on elevation of cytosolic calcium levels. There is good evidence for annexin V binding to proteins involved in signal transduction including ...
Annexins and Tissue Mineralization—Matrix Vesicles, Ion Channel Activity of Annexins and Annexin V/Collagen Interactions
Thorsten Kirsch
Physiological biomineralization is restricted to skeletal tissues and teeth. This highly complex process plays important functions during development of these tissues and it also allows these ...
Structural Conservation and Functional Versatility: Allostery as a Common Annexin Feature
Andreas Hofmann and Robert Huber
Annexin structures have been found to show a common fold due to their characteristic topology. The structural conservation within the annexin family throughout the animal, fungal and plant kin...
Interaction of Annexins with S100 Proteins
Rosario Donato
Certain annexins have the ability for form heterocomplexes with members of the Ca2+-binding S100 protein family. The predominant complex is a heterotetramer because most S100 protei...
Role of Annexin 6 in Receptor-Mediated Endocytosis, Membrane Trafficking and Signal Transduction
Thomas Grewal, Carlos Enrich and Stefan Jäckle
In recent years, the involvement of annexins in the regulation of membrane traffic has emerged as one of their predominant functions. Annexin 6 was first reported at the plasma membrane and...
Reflections on Twenty-Five Years of Annexin Research
Carl E. Creutz
This is a personal account of the discovery of synexin (annexin VII) in 1977, along with some selected observations on the development of the annexin field since that time. ...
Annexins and Phospholipases
A.G. Buckland and D.C.Wilton
The association of annexins with phospholipase A2 activity has a long history linked to the discovery of annexins I and II. As the field developed and the discovery of different gro...
The Nucleotide Face of Annexins
Joanna Bandorowicz-Pikula
This chapter provides an up-to-date summary of recent developments in the field of annexin-nucleotide interactions and their physiological significance. Since the first reports by B...
Involvement of Human Annexins in Viral Entry
Erik Depla
This review examines the role of annexins in the process of membrane trafficking in the viral life cycle. The annexins II and V have been postulated to be important molecules in the viral entr...
