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Rat annexin V crystal structure: Ca(2+)-induced conformational changes

N O Concha¹, J F Head, M A Kaetzel

¹Department of Physiology, Boston University School of Medicine, MA 02118.

Science (New York, N.Y.)

|September 3, 1993

Summary

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This study reveals how calcium binding alters rat annexin V structure. Calcium binding in domain 3 changes protein conformation, suggesting its role in membrane interactions.

Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Annexins are calcium- and phospholipid-binding proteins crucial for membrane processes.
These processes include secretion, signal transduction, and ion channel activity.

Purpose of the Study:

To determine the crystal structure of rat annexin V at high resolution.
To investigate the effect of calcium binding on annexin V conformation and function.

Main Methods:

X-ray crystallography was used to solve the crystal structure of rat annexin V.
The resolution achieved was 1.9 angstroms.
Multiple isomorphous replacement phasing was employed.

Main Results:

The crystal structure revealed calcium binding in all four domains of annexin V.

Related Experiment Videos

Calcium binding in domain 3 induced significant relocation of calcium-binding loops.

This relocation exposed a key tryptophan residue to the solvent.

Conclusions:

The observed structural alterations in annexin V suggest a functional role for domain 3.
Domain 3 may be involved in calcium-triggered interactions with phospholipid membranes.