Hyung Jun Ahn

Korea Institute of Science and Technology, Seoul, Seoul, South Korea

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Publications (3)39.44 Total impact

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    ABSTRACT: When the Z-type variant of human α(1)-antitrypsin was overexpressed in Saccharomyces cerevisiae, proteomics analysis identified YLR301w as one of the up-regulated proteins. YLR301w is a 27.5 kDa protein with no sequence homology to any known protein and has been reported to interact with Sec72 and Hrr25. The crystal structure of S. cerevisiae YLR301w has been determined at 2.3 Å resolution, revealing a novel β-structure. It consists of an N-terminal ten-stranded β-barrel with two short α-helices connected by a 23-residue linker to a seven-stranded half-barrel with two short helices at the C-terminus. The N-terminal barrel has a highly conserved hydrophobic channel that can bind hydrophobic molecules such as PEG. It forms a homodimer both in the crystal and in solution. YLR301w binds Sec72 with a K(d) of 6.2 µM, but the biological significance of this binding requires further investigation.
    Acta Crystallographica Section D Biological Crystallography 05/2012; 68(Pt 5):531-40. · 12.67 Impact Factor
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    ABSTRACT: MH5049 Novel b-structure of YLR301w from Saccharomyces cerevisiae Kim et al. Synopsis The structure of the uncharacterized protein YLR301w is reported. Queries and comments Please supply or correct as appropriate all bold underlined text. In describing corrections please refer to line numbers where appropriate: these are shown in grey. Author index Authors' names will normally be arranged alphabetically under their family name and this is commonly their last name. Prefixes (van, de etc.) will only be taken into account in the alphabetization if they begin with a capital letter. Authors wishing their names to be alphabetized differently should indicate this below. Author names may appear more than once in this list; it is not necessary to mark this correction on your proofs. AE Files: d/mh5049/mh5049.3d d/mh5049/mh5049.sgml MH5049 FA IU-1216/43(18)3 1216/42(18)3 () Printed in Singapore – all rights reserved When the Z-type variant of human 1 -antitrypsin was overexpressed in Saccharomyces cerevisiae, proteomics analysis identified YLR301w as one of the up-regulated proteins. YLR301w is a 27.5 kDa protein with no sequence homology to any known protein and has been reported to interact with Sec72 and Hrr25. The crystal structure of S. cerevisiae YLR301w has been determined at 2.3 Å resolution, revealing a novel -structure. It consists of an N-terminal ten-stranded -barrel with two short -helices connected by a 23-residue linker to a seven-stranded half-barrel with two short helices at the C-terminus. The N-terminal barrel has a highly conserved hydrophobic channel that can bind hydrophobic molecules such as PEG. It forms a homodimer both in the crystal and in solution. YLR301w binds Sec72 with a K d of 6.2 mM, but the biological significance of this binding requires further investigation.
    Acta Crystallographica Section D Biological Crystallography 01/2012; 68:531-540. · 14.10 Impact Factor
  • Acta Crystallographica Section D Biological Crystallography 01/2012; · 12.67 Impact Factor