1AXN
THE HIGH RESOLUTION STRUCTURE OF ANNEXIN III SHOWS DIFFERENCES WITH ANNEXIN V
Summary for 1AXN
| Entry DOI | 10.2210/pdb1axn/pdb |
| Descriptor | ANNEXIN III, CALCIUM ION (3 entities in total) |
| Functional Keywords | annexin family, calcium-phospholipid-binding protein complex, calcium/phospholipid-binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 36583.54 |
| Authors | Favier-Perron, B.,Lewit-Bentley, A.,Russo-Marie, F. (deposition date: 1995-08-21, release date: 1996-03-08, Last modification date: 2024-02-07) |
| Primary citation | Favier-Perron, B.,Lewit-Bentley, A.,Russo-Marie, F. The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry, 35:1740-1744, 1996 Cited by PubMed Abstract: The structure of recombinant human annexin III was solved to 1.8 A resolution. Though homologous to annexin I and V, the annexin III structure shows significant differences. The tryptophan in the calcium loop of the third domain is exposed to the solvent, as in the structure of annexin V crystallized in high calcium concentrations, although the annexin III crystals were prepared at low calcium concentrations. The position of domain III relative to the other domains is different from both annexin V and I, suggesting further flexibility of the molecule. The entire N-terminus of the protein is well-defined in the present structure. The side chain of tryptophan 5 interacts with the hinge region of the hydrophillic channel, which could have an effect on the potential mobility of this region, as well as on its possible calcium channel behavior. PubMed: 8639653DOI: 10.1021/bi952092o PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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