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Four mutants with varying degrees of thermosensitivity were characterized for their thermostability and refolding properties following incubation at the nonpermissive temperature. Structure analysis of these mutations based on the hPTP1B coordinate structure demonstrates a clear relationship between the position of each mutated amino acid relative to the catalytic cysteine residue and their thermostability. Introduction of two of these mutations in the related enzyme hPTP1B suggests that the structural defects and the resulting thermosensitivity of these mutations may represent an intrinsic property of all PTPase catalytic domains.<\/jats:p>","DOI":"10.1002\/pro.5560050405","type":"journal-article","created":{"date-parts":[[2010,7,12]],"date-time":"2010-07-12T09:02:45Z","timestamp":1278925365000},"page":"604-613","source":"Crossref","is-referenced-by-count":9,"title":["Thermosensitive mutants of the MPTP and hPTP1B protein tyrosine phosphatases: Isolation and structural analysis"],"prefix":"10.1002","volume":"5","author":[{"given":"Eric S.","family":"Muise","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alice","family":"Vrielink","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maurice 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