1ANW
THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING
Summary for 1ANW
| Entry DOI | 10.2210/pdb1anw/pdb |
| Descriptor | ANNEXIN V, CALCIUM ION (3 entities in total) |
| Functional Keywords | calcium/phospholipid-binding protein, calcium-phospholipid-binding protein complex |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 71859.34 |
| Authors | Lewit-Bentley, A.,Morera, S.,Huber, R.,Bodo, G. (deposition date: 1993-10-26, release date: 1994-12-20, Last modification date: 2024-02-07) |
| Primary citation | Lewit-Bentley, A.,Morera, S.,Huber, R.,Bodo, G. The effect of metal binding on the structure of annexin V and implications for membrane binding. Eur.J.Biochem., 210:73-77, 1992 Cited by PubMed Abstract: The structure of annexin V, crystallised in the presence of two calcium or barium ions for each protein molecule, was solved by molecular replacement to 0.24 nm resolution. The two metal ions are found in domains I and IV, i.e. on the same side of the channel that lies in the centre of the molecule. The structures of the barium and calcium form are extremely close, the only differences localised in the metal-binding sites that lie on the surface of the molecule. The occupancies of the metal ions, however, are lower for barium than for calcium, expressing the lower affinity of the protein for the former. The packing of the annexin molecules in the crystal asymmetric unit may represent a model for the calcium driven association of membrane-bound annexins that leads to membrane fusion. PubMed: 1446685DOI: 10.1111/j.1432-1033.1992.tb17392.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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