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Related Experiment Video

Updated: May 8, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

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Published on: October 2, 2017

Characterisation of CMP-sialic acid transporter substrate recognition.

Andrea Maggioni¹, Mark von Itzstein, Ingrid Bibiana Rodríguez Guzmán

¹Institute for Glycomics, Griffith University, Gold Coast Campus Queensland, 4222 (Australia).

Chembiochem : a European Journal of Chemical Biology

|September 10, 2013

Summary

Researchers identified key amino acids in the CMP-sialic acid transporter (CST) responsible for substrate specificity. This structural insight aids understanding transporter function and designing new inhibitors.

Keywords:

CMP-sialic acid transporter NMR spectroscopy nucleotide sugar transporters sialic acids site-directed mutagenesis

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Last Updated: May 8, 2026

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Area of Science:

Biochemistry
Structural Biology
Molecular Transport

Background:

CMP-sialic acid transporter (CST) is crucial for cellular sialylation.
Understanding CST substrate specificity is vital for biological processes and therapeutic development.

Purpose of the Study:

To elucidate the structural basis of CMP-sialic acid transporter (CST) substrate specificity.
To identify specific amino acid residues critical for CST function.

Main Methods:

Multidisciplinary structural analysis.
Amino acid residue identification.
Structure-function relationship studies.

Main Results:

Identified specific amino acid residues directly involved in CMP-sialic acid transporter (CST) substrate binding.
Detailed structural insights into the transporter's active site.

Conclusions:

The identified residues are key determinants of CMP-sialic acid transporter (CST) substrate specificity.
Findings contribute to understanding transporter mechanisms and designing targeted inhibitors.