2o9o
Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution
OverviewOverview
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.
About this StructureAbout this Structure
2O9O is a Single protein structure of sequence from Bubalus bubalis. This structure supersedes the now removed PDB entry 1sv8. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sun May 4 10:29:41 2008