6AHZ

The NMR Structure of the Polysialyltranseferase Domain (PSTD) in Polysialyltransferase ST8siaIV

Summary for 6AHZ

• Entry DOI: 10.2210/pdb6ahz/pdb
• NMR Information: BMRB: 36207
• Descriptor: CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase (1 entity in total)
• Functional Keywords: polysialyltransferase, polysialyltransferase domain, polysialic acid, sugar binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 4128.01

Authors

Liu, X.H.,Lu, B.,Peng, L.X.,Liao, S.M.,Zhou, F.,Chen, D.,Lu, Z.L.,Zhou, G.P.,Huang, R.B. (deposition date: 2018-08-21, release date: 2018-10-24, Last modification date: 2024-05-15)

Primary citation

Peng, L.X.,Liu, X.H.,Lu, B.,Liao, S.M.,Zhou, F.,Huang, J.M.,Chen, D.,Troy II, F.A.,Zhou, G.P.,Huang, R.B.
The Inhibition of Polysialyltranseferase ST8SiaIV Through Heparin Binding to Polysialyltransferase Domain (PSTD).
Med Chem, 15:486-495, 2019

PubMed Abstract: The polysialic acid (polySia) is a unique carbohydrate polymer produced on the surface Of Neuronal Cell Adhesion Molecule (NCAM) in a number of cancer cells, and strongly correlates with the migration and invasion of tumor cells and with aggressive, metastatic disease and poor clinical prognosis in the clinic. Its synthesis is catalyzed by two polysialyltransferases (polySTs), ST8SiaIV (PST) and ST8SiaII (STX). Selective inhibition of polySTs, therefore, presents a therapeutic opportunity to inhibit tumor invasion and metastasis due to NCAM polysialylation. Heparin has been found to be effective in inhibiting the ST8Sia IV activity, but no clear molecular rationale. It has been found that polysialyltransferase domain (PSTD) in polyST plays a significant role in influencing polyST activity, and thus it is critical for NCAM polysialylation based on the previous studies.

PubMed: 30569872
DOI: 10.2174/1573406415666181218101623

Experimental method

SOLUTION NMR