2RAN: RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES

Citation:
Abstract
Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes.
PDB ID: 2RANDownload
MMDB ID: 58190
PDB Deposition Date: 1994/9/1
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.89  Å
Source Organism:
Similar Structures:
Biological Unit for 2RAN: monomeric; determined by author
Molecular Components in 2RAN
Label Count Molecule
Protein (1 molecule)
1
Annexin V(Gene symbol: Anxa5)
Molecule annotation
Chemicals (9 molecules)
1
7
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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