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   constants in assessing the conformational behavior of carbohydrates. A
   discussion of conformational studies of oligosaccharides in solution
   and in the protein-bound state is described. Literature data on the
   structures and syntheses of muropeptides, proteins interacting with
   peptidoglycans, and the structures of peptidoglycan complexes with
   muropeptides are also reviewed. Glycopeptide antibiotics represent the
   last line of defense against the often lethal Gram-positive bacterial
   infections. The different point of views of solution and solid-state
   NMR, X-ray crystallography, and molecular dynamics simulation of this
   antibiotic family is compared in the last part of this review.
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   [68]Journal of Molecular Biology
   [69]Volume 288, Issue 3, 7 May 1999, Pages 403-412
     __________________________________________________________________

   [70]doi:10.1006/jmbi.1999.2693 | [71]How to Cite or Link Using DOI
   Copyright © 1999 Academic Press. All rights reserved.
     [72]Permissions & Reprints

 §4§  Regular article §4§

   Crystal structure of cyanovirin-N, a potent HIV-inactivating protein,
   shows unexpected domain swapping [73]^1

   Fan Yang [74]^1, Carole A. Bewley [75]^2, John M. Louis [76]^2, Kirk R.
   Gustafson [77]^3, Michael R. Boyd [78]^3, Angela M. Gronenborn [79]^2,
   G. Marius Clore [80]^2 and Alexander Wlodawer [81]^1^,
   [82]^Corresponding Author Contact Information ^, [83]^E-mail The
   Corresponding Author

   ^1 Macromolecular Structure Laboratory, ABL-Basic Research Program,
   NCI-Frederick Cancer Research and Development Center, Frederick, MD
   21702-1201, USA

   ^2 Laboratory of Chemical Physics, National Institute of Diabetes and
   Digestive and Kidney Diseases, National Institutes of Health, Bethesda
   MD 20892-0520, USA

   ^3 Laboratory of Drug Discovery Research and Development DTP,
   NCI-Frederick Cancer Research and Development Center, Frederick, MD
   21702-1201, USA
   Received 15 December 1998;
   Revised 4 March 1999;
   accepted 4 March 1999.
   Available online 2 May 2002.

 §3§ Abstract §3§

   The crystal structure of cyanovirin-N (CV-N), a protein with potent
   antiviral activity, was solved at 1.5 Å resolution by molecular
   replacement using as the search model the solution structure previously
   determined by NMR. The crystals belong to the space group P3[2]21 with
   one monomer of CV-N in each asymmetric unit. The primary structure of
   CV-N contains 101 residues organized in two domains, A (residues 1 to
   50) and B (residues 51 to 101), with a high degree of internal sequence
   and structural similarity. We found that under the conditions of the
   crystallographic experiments (low pH and 26 % isopropanol), two
   symmetrically related monomers form a dimer by domain swapping, such
   that domain A of one monomer interacts with domain B′ of its
   crystallographic symmetry mate and vice versa. Because the two swapped
   domains are distant from each other, domain swapping does not result in
   additional intramolecular interactions. Even though one of the protein
   sample solutions that was used for crystallization clearly contained
   100 % monomeric CV-N molecules, as judged by various methods, we were
   only able to obtain crystals containing domain-swapped dimers. With the
   exception of the unexpected phenomenon of domain swapping, the crystal
   structure of CV-N is very similar to the NMR structure, with a
   root-mean-square deviation of 0.55 Å for the main-chain atoms, the best
   agreement reported to date for structures solved using both techniques.

   Author Keywords: Author Keywords: human immunodeficiency virus;
   virucides; cyanovirin-N; domain swapping; protein structure
   CV-N, cyanovirin N; HIV, human immunodeficiency virus; PBS,
   phosphate-buffered saline; IL-10, interleukin-10

 §3§ Article Outline §3§

   [84]• Introduction

   [85]• Results

   [86]• Discussion

   [87]• Materials and methods
          [88]• Protein Data Bank accession numbers

   [89]• Acknowledgements

   [90]• References

 §3§ Introduction §3§