Fold-recognition and comparative modeling of human α2,3-sialyltransferases reveal their sequence and structural similarities to CstII from Campylobacter jejuni
2006

Modeling Human Sialyltransferases

publication Evidence: moderate

Author Information

Author(s): Sujatha MS, Balaji Petety V

Primary Institution: Indian Institute of Technology Bombay

Hypothesis

The objective of the current work is to model the 3-D structures of human SiaTs which transfer the sialic acid in α2,3-linkage.

Conclusion

The modeled 3-D structures can be used for docking and other modeling studies and for the rational identification of residues to be mutated to impart desired properties.

Supporting Evidence

  • The modeled structures have acceptable stereochemical properties.
  • The study illustrates the difficulties in modeling specific proteins of interest.
  • The results establish a sequence/structure relationship between sialyltransferases of two distinct families.

Takeaway

Scientists created 3-D models of specific proteins that help in transferring sugar molecules, which can be used to understand how to change these proteins for better functions.

Methodology

The 3-D structures of six human SiaTs were modeled using fold-recognition and comparative modeling methods.

Limitations

The fold-recognition servers could not find a template for certain regions, and some regions were not modeled.

Digital Object Identifier (DOI)

10.1186/1472-6807-6-9

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