1lom
From Proteopedia
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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 with SO4 and CA as ligands. 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 Thu Nov 8 14:17:24 2007
Categories: Nostoc ellipsosporum | Single protein | Botos, I. | Boyd, M.R. | Cartner, L.K. | Mori, T. | Wlodawer, A. | CA | SO4 | Cyanovirin-n | Domain-swapping | Gp120 | Hiv-inactivating
