Structural highlights
Publication Abstract from PubMed
The lectin from the seeds of snake gourd (Trichosanthes anguina) has been crystallized in two forms using the hanging-drop method. Both the forms are hexagonal, with the asymmetric unit containing one subunit consisting of two polypeptide chains linked through disulfide bridges. Intensity data from one of the forms were collected at room temperature as well as at low temperature to 3 A resolution. Molecular-replacement studies indicate that the lectin is homologous to type II ribosome-inactivating proteins. Partial refinement confirms this conclusion.
Crystallization and preliminary X-ray studies of snake gourd lectin: homology with type II ribosome-inactivating proteins.,Manoj N, Jeyaprakash AA, Pratap JV, Komath SS, Kenoth R, Swamy MJ, Vijayan M Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):912-4. Epub 2001 May 25. PMID:11375527[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Manoj N, Jeyaprakash AA, Pratap JV, Komath SS, Kenoth R, Swamy MJ, Vijayan M. Crystallization and preliminary X-ray studies of snake gourd lectin: homology with type II ribosome-inactivating proteins. Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):912-4. Epub 2001 May 25. PMID:11375527
