1l5e | pdb_00001l5e

The domain-swapped dimer of CV-N in solution

spinqualitylabelsall models 1l5e Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1l5e is a 2 chain structure with sequence from Nostoc ellipsosporum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 1 model 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 The structure of the potent HIV-inactivating protein cyanovirin-N was previously found by NMR to be a monomer in solution and a domain-swapped dimer by X-ray crystallography. Here we demonstrate that, in solution, CV-N can exist both in monomeric and in domain-swapped dimeric form. The dimer is a metastable, kinetically trapped structure at neutral pH and room temperature. Based on orientational NMR constraints, we show that the domain-swapped solution dimer is similar to structures in two different crystal forms, exhibiting solely a small reorientation around the hinge region. Mutation of the single proline residue in the hinge to glycine significantly stabilizes the protein in both its monomeric and dimeric forms. By contrast, mutation of the neighboring serine to proline results in an exclusively dimeric protein, caused by a drastic destabilization of the monomer. The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.,Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM Structure. 2002 May;10(5):673-86. PMID:12015150 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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