Title : Interaction of collagen-like peptide models of asymmetric acetylcholinesterase with glycosaminoglycans: spectroscopic studies of conformational changes and stability.

Pub. Date : 2000 Dec 5

PMID : 11101304






3 Functional Relationships(s)
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1 The effect of heparin on the conformation and stability of triple-helical peptide models of the collagen tail of asymmetric acetylcholinesterase expands our understanding of heparin interactions with proteins and presents an opportunity for clarifying the nature of binding of ligands to collagen triple-helix domains. Heparin acetylcholinesterase (Cartwright blood group) Homo sapiens
2 The effect of heparin on the conformation and stability of triple-helical peptide models of the collagen tail of asymmetric acetylcholinesterase expands our understanding of heparin interactions with proteins and presents an opportunity for clarifying the nature of binding of ligands to collagen triple-helix domains. Heparin acetylcholinesterase (Cartwright blood group) Homo sapiens
3 Within the collagen tail of AChE, there are two consensus sequences for heparin binding of the form BBXB, surrounded by additional basic residues. Heparin acetylcholinesterase (Cartwright blood group) Homo sapiens