Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Published online before print October 26, 2007, 10.1110/ps.073157507
Protein Science (2007), 16:2756-2760. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
ps.073157507v1
16/12/2756    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moulaei, T.
Right arrow Articles by Wlodawer, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moulaei, T.
Right arrow Articles by Wlodawer, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

PROTEIN STRUCTURE REPORT

Atomic-resolution crystal structure of the antiviral lectin scytovirin

Tinoush Moulaei1, Istvan Botos1,5, Natasza E. Ziólkowska1,6, Heidi R. Bokesch2,3, Lauren R. Krumpe2,3, Tawnya C. McKee2, Barry R. O'Keefe2, Zbigniew Dauter4, and Alexander Wlodawer1

1 Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI-Frederick, Frederick, Maryland 21702-1201, USA
2 Molecular Targets Development Program, Center for Cancer Research, National Cancer Institute, NCI-Frederick, Frederick, Maryland 21702-1201, USA
3 SAIC-Frederick Inc., National Cancer Institute, Frederick, Maryland 21702-1201, USA
4 Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne National Laboratory, Argonne, Illinois 60439, USA

(RECEIVED August 2, 2007; FINAL REVISION September 6, 2007; ACCEPTED September 7, 2007)

The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single-wavelength anomalous scattering and refined with data extending to 1.3 Å and 1.0 Å resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 Å for 40 pairs of C{alpha} atoms). The crystal structure differs significantly from a previously published NMR structure of the same protein, with the RMS deviations calculated separately for the N- and C-terminal domains of 5.3 Å and 3.7 Å, respectively, and a very different relationship between the two domains. In addition, the disulfide bonding pattern of the crystal structures differs from that described in the previously published mass spectrometry and NMR studies.

Keywords: lectins; new fold; anomalous scattering; scytovirin


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2007 by The Protein Society.