Structural analysis and unique molecular recognition properties of a Bauhinia forficata lectin that inhibits cancer cell growth
Lectins have been used at length for basic research and clinical applications. New insights into the molecular recognition properties enhance our basic understanding of carbohydrate-protein interactions and aid in the design/development of new lectins. In this study, we used a combination of cell-ba...
| Authors: | , , , , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2017 |
| Country: | Brasil |
| Institution: | Universidade Federal de São Paulo (UNIFESP) |
| Repository: | Repositório Institucional da UNIFESP |
| Language: | English |
| OAI Identifier: | oai:repositorio.unifesp.br:11600/55199 |
| Online Access: | http://dx.doi.org/10.1111/febs.13989 https://repositorio.unifesp.br/handle/11600/55199 |
| Access Level: | Open access |
| Keyword: | cancer cell growth inhibition carbohydrate binding crystal structure lectin Tn antigen |
| Summary: | Lectins have been used at length for basic research and clinical applications. New insights into the molecular recognition properties enhance our basic understanding of carbohydrate-protein interactions and aid in the design/development of new lectins. In this study, we used a combination of cell-based assays, glycan microarrays, and X-ray crystallography to evaluate the structure and function of the recombinant Bauhinia forficata lectin (BfL). The lectin was shown to be cytostatic for several cancer cell lines included in the NCI-60 panel |
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