1lom is a 1 chain structure with sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A. Domain-swapped structure of a mutant of cyanovirin-N. Biochem Biophys Res Commun. 2002 May 31;294(1):184-90. PMID:12054761 doi:10.1016/S0006-291X(02)00455-2
