Lead poisoning has been identified as one of the most common preventable health concerns in the U.S.  The exact way each biological system is affected is still unknown; therefore treatment for lead poisoning is till inadequate.  Various metalloproteins, such as the membrane trafficking protein synaptotagmin I (syt1), have been shown to bind lead with a greater affinity than their native metal ion and have been identified as a potential target of lead.  Since the function of biological macromolecules is dictated by their structure, changes in the structure of syt1 upon lead binding may be responsible for the loss in function of this protein.  Here we report various structural studies of syt1 in the presence of lead and it's native calcium ions.  With a better understanding of the structural differences of metal bound syt1 we aim to increase what is known regarding the role(s) of lead in lead poisoning.

Structural characterization of lead bound Synaptogmin I

243rd National Meeting (2012)

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