1lom: Difference between revisions
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'''CYANOVIRIN-N DOUBLE MUTANT P51S S52P''' | '''CYANOVIRIN-N DOUBLE MUTANT P51S S52P''' | ||
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[[Category: Mori, T.]] | [[Category: Mori, T.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: | [[Category: Cyanovirin-n]] | ||
[[Category: | [[Category: Domain-swapping]] | ||
[[Category: | [[Category: Gp120]] | ||
[[Category: | [[Category: Hiv-inactivating]] | ||
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Revision as of 21:07, 2 May 2008
CYANOVIRIN-N DOUBLE MUTANT P51S S52P
Overview
Cyanovirin-N (CV-N) is a potent 11 kDa HIV-inactivating protein that binds with high affinity to the HIV surface envelope protein gp120. A double mutant P51S/S52P of CV-N was engineered by swapping two critical hinge-region residues Pro51 and Ser52. This mutant has biochemical and biophysical characteristics equivalent to the wild-type CV-N and its structure resembles that of wild-type CV-N. However, the mutant shows a different orientation in the hinge region that connects two domains of the protein. The observation that this double mutant crystallizes under a wide variety of conditions challenges some of the current hypotheses on domain swapping and on the role of hinge-region proline residues in domain orientation. The current structure contributes to the understanding of domain swapping in cyanovirins, permitting rational design of domain-swapped CV-N mutants.
About this Structure
1LOM is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
Domain-swapped structure of a mutant of cyanovirin-N., Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A, Biochem Biophys Res Commun. 2002 May 31;294(1):184-90. PMID:12054761 Page seeded by OCA on Sat May 3 00:07:20 2008
