1lom

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Revision as of 12:11, 8 November 2007

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spinqualitylabelsall models 1lom, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

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