1lom | pdb_00001lom

CYANOVIRIN-N DOUBLE MUTANT P51S S52P

spinqualitylabelsall models 1lom, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lom is a 1 chain structure with sequence from Anabaena variabilis var. ellipsospora. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, SO4 Related: 3ezm, 1l5b, 1l5e Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CVN_NOSEL] Mannose-binding lectin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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