Taxonomic distribution of proteins containing ANX domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing ANX domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Calcium binding and conformational response in EF-hand proteins.

Ikura M
Trends Biochem Sci. 1996; 21: 14-7

EF-hand proteins undergo conformational changes upon binding of Ca2+. This event is a crucial step in many Ca2+-dependent cellular processes. Recent advances in the three-dimensional structural analysis of various EF-hand proteins have led to new insights into the structure and functional relationship of this large family of Ca2+-binding proteins.

Annexin homologues in Giardia lamblia.

Fiedler K, Simons K
Trends Biochem Sci. 1995; 20: 177-8

Structural evolution of the annexin supergene family.

Smith PD, Moss SE
Trends Genet. 1994; 10: 241-6

The annexin family of calcium-binding proteins is comprised of at least ten mammalian genes, with additional representatives in lower eukaryotes. Recent structural analyses of several annexin genes have provided insights into the relationship between exon organization and functional domains. We discuss the implications of these findings and speculate on the evolutionary origins of the annexin supergene family.

The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes.

Huber R, Romisch J, Paques EP
EMBO J. 1990; 9: 3867-74

Human annexin V (PP4), a member of the family of calcium, membrane binding proteins, has been crystallized in the presence of calcium and analysed by crystallography by multiple isomorphic replacement at 3 A and preliminarily refined at 2.5 A resolution. The molecule has dimensions of 64 x 40 x 30 A3 and is folded into four domains of similar structure. Each domain consists of five alpha-helices wound into a right-handed superhelix yielding a globular structure of approximately 18 A diameter. The domains have hydrophobic cores whose amino acid sequences are conserved between the domains and within the annexin family of proteins. The four domains are folded into an almost planar array by tight (hydrophobic) pair-wise packing of domains II and III and I and IV to generate modules (II-III) and (I-IV), respectively. The assembly is symmetric with three parallel approximate diads relating II to III, I to IV and the module (II-III) to (I-IV), respectively. The latter diad marks a channel through the centre of the molecule coated with charged amino acid residues. The protein has structural features of channel forming membrane proteins and a polar surface characteristic of soluble proteins. It is a member of the third class of amphipathic proteins different from soluble and membrane proteins.