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PMID: 2834230 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins.

FEBS letters ·Vol. 231 ·No. 1 ·1988-04-11 ·Pages 51-3

Petersen TE

Abstract

Amino acid sequence alignment of the amino-terminal of thrombomodulin and pancreatic stone protein with the hepatic asialoglycoprotein receptor shows that these proteins are homologous. From the known disulfide bridge pattern of other proteins belonging to the same family two disulfide bonds can be predicted. The homology raises the question whether the amino-terminal part of thrombomodulin and the pancreatic protein binds carbohydrate or perhaps like tetranectin have a specific affinity for other proteins.

MeSH Terms
Amino Acid Sequence Animals Asialoglycoprotein Receptor Calcium-Binding Proteins/genetics Humans Lithostathine Molecular Sequence Data Nerve Tissue Proteins Phosphoproteins/genetics Receptors, Cell Surface/genetics Receptors, Immunologic/genetics Receptors, Thrombin Sequence Homology, Nucleic Acid Species Specificity Thrombin/metabolism
Chemicals
Asialoglycoprotein Receptor Calcium-Binding Proteins Lithostathine Nerve Tissue Proteins Phosphoproteins REG1A protein, human Receptors, Cell Surface Receptors, Immunologic Receptors, Thrombin Thrombin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Petersen T E
Department of Molecular Biology and Plant Physiology, University of Aarhus, Denmark.
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1988-04-11
Pages
51-3
Language
English
Region
England
NLM ID
0155157
Subset
IM
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