THE STRUCTURE OF FULL LENGTH HUMAN ANNEXIN I IN COMPLEX WITH CALCIUM AND PHOSPHA

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Annexins are soluble proteins that bind to negatively charged phospholipids in a calcium dependent manner. Each member of the annexin family comprises of two principal domains: a conserved carboxyl terminal protein core and an amino terminal that is unique for a given member of the family that may specify individual annexin properties. Several high-resolution crystal annexin structures have been solved (including annexin I); however, none of the published annexin structures contain a complete N-terminal domain. Currently, we have been able to express, purify and crystallize full length human annexin I. By solving the structure of the full length human annexin I we hope to get more information on how the N-terminal domain interacts with the core domain. In addition, we hope to gain some useful insights on how this member of the annexin family is implicated in membrane related processes including membrane aggregation and fusion. We propose that the structural conformation of human annexin I will be altered in the presence of calcium and phosphate ions. We wish to test whether this structural conformational change occurs by not only solving the structure of native full length human annexin I, but also solving the full length human annexin I in the presence of calcium and phosphate ions