Structural highlights
Function
[G4V4F9_CUPSA] Has a role in the innate immune system.[1]
Publication Abstract from PubMed
Cupiennius salei single insulin-like growth factor binding domain protein (SIBD-1) is an 8.6 kDa Cys-, Pro-, and Gly-rich protein, discovered in the hemocytes of the Central American hunting spider Cupiennius salei. SIBD-1 exhibits high sequence similarity to the N-terminal domain of the insulin-like growth factor-binding protein superfamily and has been reported to play an important role in the spider's immune system. Here, the recombinant expression as well as the elucidation of the three dimensional structure of recombinant SIBD-1 and the characterization of the sugar moiety at Thr2 of native SIBD-1 is described in detail. Proteins 2012. (c) 2012 Wiley-Liss, Inc.
Structural and Biochemical Characterization of Native and Recombinant Single Insulin-like Growth Factor-Binding Domain Protein (SIBD-1) from the Central American Hunting Spider Cupiennius salei (Ctenidae).,Trachsel C, Widmer C, Kampfer U, Buhr C, Baumann T, Kuhn-Nentwig L, Schurch S, Schaller J, Baumann U Proteins. 2012 May 24. doi: 10.1002/prot.24119. PMID:22622866[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuhn-Nentwig L, Largiader CR, Streitberger K, Chandru S, Baumann T, Kampfer U, Schaller J, Schurch S, Nentwig W. Purification, cDNA structure and biological significance of a single insulin-like growth factor-binding domain protein (SIBD-1) identified in the hemocytes of the spider Cupiennius salei. Insect Biochem Mol Biol. 2011 Nov;41(11):891-901. doi:, 10.1016/j.ibmb.2011.08.003. Epub 2011 Aug 26. PMID:21888974 doi:http://dx.doi.org/10.1016/j.ibmb.2011.08.003
- ↑ Trachsel C, Widmer C, Kampfer U, Buhr C, Baumann T, Kuhn-Nentwig L, Schurch S, Schaller J, Baumann U. Structural and Biochemical Characterization of Native and Recombinant Single Insulin-like Growth Factor-Binding Domain Protein (SIBD-1) from the Central American Hunting Spider Cupiennius salei (Ctenidae). Proteins. 2012 May 24. doi: 10.1002/prot.24119. PMID:22622866 doi:10.1002/prot.24119
