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PMID: 3801003 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Characterization of sites of tyrosine sulfation in proteins and criteria for predicting their occurrence.

Biochemical and biophysical research communications ·Vol. 141 ·No. 1 ·1986-11-26 ·Pages 326-33

Hortin G, Folz R, Gordon JI, Strauss AW

Abstract

A wide variety of secretory proteins have recently been found to undergo post-translational sulfation of specific tyrosine residues. Here, amino acid sequences surrounding known sulfation sites in proteins are analyzed in order to identify factors which determine the specificity of sulfation. Several distinctive features of sulfation sites are identified, including: abundance of acidic amino acid residues, lack of basic residues, low hydropathy, absence of neighboring cysteine residues, lack of extended secondary structure. Rules are proposed for predicting likely sites of sulfation based on the amino acid sequence of a protein.

MeSH Terms
Amino Acid Sequence Protein Conformation Protein Processing, Post-Translational Proteins/metabolism Solubility Structure-Activity Relationship Sulfates/metabolism Tyrosine/metabolism
Chemicals
Proteins Sulfates Tyrosine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hortin G
Folz R
Gordon J I
Strauss A W
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1986-11-26
Pages
326-33
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NIGMS NIH HHS · GM-07200 · United States
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