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Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping.

Abstract：

:The crystal structure of cyanovirin-N (CV-N), a protein with potent antiviral activity, was solved at 1.5 A resolution by molecular replacement using as the search model the solution structure previously determined by NMR. The crystals belong to the space group P3221 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 A for the main-chain atoms, the best agreement reported to date for structures solved using both techniques.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Yang F,Bewley CA,Louis JM,Gustafson KR,Boyd MR,Gronenborn AM,Clore GM,Wlodawer A

doi

10.1006/jmbi.1999.2693

keywords:

subject

Has Abstract

pub_date

1999-05-07 00:00:00

pages

403-12

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)92693-1

journal_volume

288

pub_type

杂志文章

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