2RAN

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

Summary for 2RAN

Entry DOI	10.2210/pdb2ran/pdb
Descriptor	ANNEXIN V, CALCIUM ION, SULFATE ION, ... (4 entities in total)
Functional Keywords	calcium/phospholipid-binding protein, calcium-phospholipid-binding protein complex
Biological source	Rattus norvegicus (Norway rat)
Total number of polymer chains	1
Total formula weight	35899.76
Authors	Concha, N.O.,Head, J.F.,Kaetzel, M.A.,Dedman, J.R.,Seaton, B.A. (deposition date: 1994-09-01, release date: 1994-11-30, Last modification date: 2024-02-21)
Primary citation	Concha, N.O.,Head, J.F.,Kaetzel, M.A.,Dedman, J.R.,Seaton, B.A. Rat annexin V crystal structure: Ca(2+)-induced conformational changes. Science, 261:1321-1324, 1993 Cited by PubMed 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. PubMed: 8362244 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.89 Å)

Structure validation