1l5e
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(New page: 200px<br /><applet load="1l5e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5e" /> '''The domain-swapped dimer of CV-N in solution...)
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Revision as of 18:09, 20 November 2007
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The domain-swapped dimer of CV-N in solution
Overview
The structure of the potent HIV-inactivating protein cyanovirin-N was, previously found by NMR to be a monomer in solution and a domain-swapped, dimer by X-ray crystallography. Here we demonstrate that, in solution, CV-N can exist both in monomeric and in domain-swapped dimeric form. The, dimer is a metastable, kinetically trapped structure at neutral pH and, room temperature. Based on orientational NMR constraints, we show that the, domain-swapped solution dimer is similar to structures in two different, crystal forms, exhibiting solely a small reorientation around the hinge, region. Mutation of the single proline residue in the hinge to glycine, significantly stabilizes the protein in both its monomeric and dimeric, forms. By contrast, mutation of the neighboring serine to proline results, in an exclusively dimeric protein, caused by a drastic destabilization of, the monomer.
About this Structure
1L5E is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures., Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM, Structure. 2002 May;10(5):673-86. PMID:12015150
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