@misc{10481/87304,
year = {2011},
month = {9},
url = {https://hdl.handle.net/10481/87304},
abstract = {ICA512 (or IA-2) is a transmembrane protein-tyrosine phosphatase located in secretory granules of neuroendocrine cells.
Initially, it was identified as one of the main antigens of autoimmune diabetes. Later, it was found that during insulin
secretion, the cytoplasmic domain of ICA512 is cleaved and relocated to the nucleus, where it stimulates the transcription of
the insulin gene. The role of the other parts of the receptor in insulin secretion is yet to be unveiled. The structures of the
intracellular pseudocatalytic and mature extracellular domains are known, but the transmembrane domain and several
intracellular and extracellular parts of the receptor are poorly characterized. Moreover the overall structure of the receptor
remains to be established. We started to address this issue studying by X-ray crystallography the structure of the mature
ectodomain of ICA512 (ME ICA512) and variants thereof. The variants and crystallization conditions were chosen with the
purpose of exploring putative association interfaces, metal binding sites and all other structural details that might help, in
subsequent works, to build a model of the entire receptor. Several structural features were clarified and three main different
association modes of ME ICA512 were identified. The results provide essential pieces of information for the design of new
experiments aimed to assess the structure in vivo.},
publisher = {Plos One . PLoS (Public Library of Science)},
title = {Protein-Protein Interactions in Crystals of the Human Receptor-Type Protein Tyrosine Phosphatase ICA512 Ectodomain},
doi = {10.1371/journal.pone.0024191},
author = {Primo, María E. and Jakancic, Jean and Noguera, Martín E. and Risso, Valeria Alejandra and Sosa, Laura and Sica, Mauricio P. and Solimena, Michele and Poskus, Edgardo and Ermácora, Mario R.},
}