Document Detail

Structural and biochemical characterization of the N-terminal domain of flocculin Lg-Flo1p from Saccharomyces pastorianus reveals a unique specificity for phosphorylated mannose.
MedLine Citation:
PMID:  23281814     Owner:  NLM     Status:  MEDLINE    
DATABASE: Structural data have been deposited in the Protein Data Bank under accession number 4GQ7.
Lyann Sim; Magnus Groes; Kjeld Olesen; Anette Henriksen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-01-24
Journal Detail:
Title:  The FEBS journal     Volume:  280     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-18     Completed Date:  2013-04-11     Revised Date:  2013-05-20    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  1073-83     Citation Subset:  IM    
Copyright Information:
© 2013 The Authors Journal compilation © 2013 FEBS.
The Protein Chemistry Group, Carlsberg Laboratory, Copenhagen, Denmark.
Data Bank Information
Bank Name/Acc. No.:
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MeSH Terms
Amino Acid Sequence
Binding Sites
Calcium / chemistry
Conserved Sequence
Crystallography, X-Ray
Fungal Proteins / chemistry*
Glucosephosphates / chemistry
Hydrogen-Ion Concentration
Mannose-Binding Lectins / chemistry*
Mannosephosphates / chemistry*
Models, Molecular
Molecular Sequence Data
Osmolar Concentration
Protein Binding
Protein Structure, Tertiary
Structural Homology, Protein
Substrate Specificity
Surface Properties
Reg. No./Substance:
0/Fungal Proteins; 0/Glucosephosphates; 0/Mannose-Binding Lectins; 0/Mannosephosphates; 27251-84-9/mannose 1-phosphate; 7440-70-2/Calcium; CIX3U01VAU/glucose-1-phosphate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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