1LOM

CYANOVIRIN-N DOUBLE MUTANT P51S S52P

Summary for 1LOM

• Entry DOI: 10.2210/pdb1lom/pdb
• Related: 1L5B 1L5E 3EZM
• Descriptor: Cyanovirin-N, SULFATE ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: cyanovirin-n, domain-swapping, hiv-inactivating, gp120, antiviral protein
• Biological source: Nostoc ellipsosporum
• Total number of polymer chains: 1
• Total formula weight: 11198.31

Authors

Botos, I.,Mori, T.,Cartner, L.K.,Boyd, M.R.,Wlodawer, A. (deposition date: 2002-05-06, release date: 2002-06-26, Last modification date: 2024-10-30)

Primary citation

Botos, I.,Mori, T.,Cartner, L.K.,Boyd, M.R.,Wlodawer, A.
Domain-swapped structure of a mutant of cyanovirin-N.
Biochem.Biophys.Res.Commun., 294:184-190, 2002

PubMed Abstract: 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.

PubMed: 12054761
DOI: 10.1016/S0006-291X(02)00455-2

Experimental method

X-RAY DIFFRACTION (1.72 Å)