2o9o

Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution

spinqualitylabelsall models 2o9o, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2o9o is a 1 chain structure with sequence from Bubbu. This structure supersedes the now removed PDB entry 1sv8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MAN, NAG Related: 2esc, 2dpe Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CH3L1_BUBBU] Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment (By similarity). 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 crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 A resolution. SPB-40 acts as a protective signalling factor by binding to viable cells during the early phase of involution, during which extensive tissue remodelling occurs. It was isolated from the dry secretions of Murrah buffalo. It was purified and crystallized using the hanging-drop vapour-diffusion method with 19% ethanol as the precipitant. The protein was also cloned and its complete nucleotide and amino-acid sequences were determined. When compared with the sequences of other members of the family, the sequence of SPB-40 revealed two very important mutations in the sugar-binding region, in which Tyr120 changed to Trp120 and Glu269 changed to Trp269. The structure showed a significant distortion in the shape of the sugar-binding groove. The water structure in the groove is also drastically altered. The folding of the protein chain in the flexible region comprising segments His188-His197, Phe202-Arg212 and Tyr244-Pro260 shows large variations when compared with other proteins of the family. Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution.,Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):258-65. Epub 2007 Mar 12. PMID:17401190 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chitinase-3-like protein 3D structures

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