3hp8

Crystal structure of a designed Cyanovirin-N homolog lectin; LKAMG, bound to sucrose

spinqualitylabelsall models 3hp8, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hp8 is a 2 chain structure with sequence from Neurospora crassa and Tuber borchii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: DTT, FRU, GLC, PRD_900003 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CVNH_NEUCR Mannose-binding lectin. CVNH_TUBBO 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 NMR and X-ray structures of a designed chimeric cyanovirin-N homolog (CVNH) protein were determined. The individual halves of the structure are similar to their counterparts in the parent proteins, with domains A and B resembling the structures of TbCVNH and NcCVNH, respectively. No significant differences between the solution and crystal conformations were observed, although details in loop conformations and distinct crystal packing-induced features are present. Carbohydrate binding studies by NMR revealed affinity and specificity for Glc alpha(1-2)Frc and Man alpha(1-2)Man, and the parental half that is devoid of any sucrose affinity in NcCVNH was transformed into a genuine sucrose binding site in the context of the chimera. The atomic details of sugar recognition are seen in the crystal structure of the protein with two bound Glc alpha(1-2)Frc molecules. Both sugars exhibit different conformations around the glycosidic bond and engage in unique hydrogen bonding networks in the two sites. Although the protein is able to bind two Man alpha(1-2)Man molecules, a property associated with HIV-inactivation, no anti-HIV activity was observed for the hybrid protein. These results provide the structural basis for sugar recognition in the CVNH family and aid in deciphering the relationship between sugar binding and anti-HIV activity. A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding.,Koharudin LM, Furey W, Gronenborn AM Proteins. 2009 Dec;77(4):904-15. PMID:19639634 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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