Document Detail

In silico study of human aquaporin AQP11 and AQP12 channels.
MedLine Citation:
PMID:  23359558     Owner:  NLM     Status:  MEDLINE    
AQP11 and AQP12 are the most distantly related paralogs of the aquaporin family in human. They share indeed a low sequence similarity with other aquaporins and exhibit a modified N-terminal NPA signature motif. Furthermore, they have an anomalous subcellular localization. The AQP11 and AQP12 biological role remains to be fully clarified and their ability to allow transport of water is still debated. We have built accurate 3D-models for AQP11 and AQP12 and comprehensively compared their sequence and structure to other known aquaporins. In order to investigate whether they appear compatible or not with water permeability, we especially focused on the amino acid composition and electrostatics of their channels, keeping the structure of the low-water efficiency AQP0 as a reference system. Our analysis points out a possible alternative ar/R site and shows that these aquaporins feature unique residues at key pore-lining positions that make the shape, composition and electrostatics of their channel peculiar. Such residues can represent pivotal hints to study and explain the AQP11 and AQP12 biological and molecular function.
Luisa Calvanese; Marialuisa Pellegrini-Calace; Romina Oliva
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-02-26
Journal Detail:
Title:  Protein science : a publication of the Protein Society     Volume:  22     ISSN:  1469-896X     ISO Abbreviation:  Protein Sci.     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-03-20     Completed Date:  2013-08-26     Revised Date:  2014-04-01    
Medline Journal Info:
Nlm Unique ID:  9211750     Medline TA:  Protein Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  455-66     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 The Protein Society.
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MeSH Terms
Amino Acid Sequence
Aquaporins / chemistry*
Computational Biology
Computer Simulation
Cysteine / chemistry
Models, Molecular
Molecular Sequence Data
Protein Conformation
Sequence Alignment
Static Electricity
Water / chemistry
Reg. No./Substance:
0/AQP11 protein, human; 0/Aquaporins; 0/aquaporin 12, human; 059QF0KO0R/Water; K848JZ4886/Cysteine

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

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