Publication Details (including relevant citation information):
Proteins (2010) 78: 1992-1998.
Parthasarathy Sampathkumar, Sinem A. Ozyurt, Johnny Do, Kevin T. Bain, Mark Dickey, Logan A. Rodgers, Tarun Gheyi, Andrej Sali, Seung Joong Kim, Jeremy Phillips, Ursula Pieper, Javier Fernandez-Martinez, Josef D. Franke, Anne Martel, Hiro Tsuruta, Shane Atwell, Devon A. Thompson, J. Spencer Emtage, Stephen R. Wasserman, Michael P. Rout, J. Michael Sauder, Stephen K. Burley
As a part of ongoing efforts at the New York SGX Research Center for Structural Genomics (www.nysgxrc.org) to determine crystal structures of distinct components of the yeast nuclear pore complex (NPC), we report herein structures of Nup145N residues 443-605 [Nup145N(443-605)] from the larger autoproteolytic segment. The monomeric architecture of Nup145N(443-605) is similar to that of the autoproteolytic domain of human Nup98-N and the homologous domain of Nup116. In contrast, Nup145N(443-605) and Nup98-N show different modes of association in the crystalline state. Results of Small Angle X-ray Scattering (SAXS) in solution are consistent with the head-to-tail dimer of Nup145N(443-605), observed in two different crystal forms.