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Structure and Function of a Model Member of the SulP Transporter Family

Loughlin, Patrick; Shelden, Megan; Tierney, Mary (Louise); Howitt, Susan

Description

SHST1 is a sulfate transporter that belongs to a large and diverse family of anion transporters. Little is known about the structure and function of any member of the family. Site-directed mutagenesis of SHST1 is being used to understand the function of particular amino acids. We have mutated highly conserved amino acid residues and the results suggest that the first two helices play an important role in the transport pathway. Furthermore, mutation of equivalent residues to those altered in...[Show more]

dc.contributor.authorLoughlin, Patrick
dc.contributor.authorShelden, Megan
dc.contributor.authorTierney, Mary (Louise)
dc.contributor.authorHowitt, Susan
dc.date.accessioned2015-12-13T23:24:46Z
dc.identifier.issn1085-9195
dc.identifier.urihttp://hdl.handle.net/1885/92375
dc.description.abstractSHST1 is a sulfate transporter that belongs to a large and diverse family of anion transporters. Little is known about the structure and function of any member of the family. Site-directed mutagenesis of SHST1 is being used to understand the function of particular amino acids. We have mutated highly conserved amino acid residues and the results suggest that the first two helices play an important role in the transport pathway. Furthermore, mutation of equivalent residues to those altered in human genetic diseases produces deleterious effects in SHST1. These results suggest that there are similarities in the molecular mechanism of transport throughout the family and the information obtained with SHST1 may be applicable to the entire family.
dc.publisherHumana Press Inc.
dc.sourceCell Biochemistry and Biophysics
dc.subjectKeywords: amino acid; carrier protein; sulfate; vegetable protein; amino acid sequence; chemical model; chemistry; legume; metabolism; molecular genetics; nucleotide sequence; protein secondary structure; review; site directed mutagenesis; structure activity relati Congenital chloride diarrhea; Diastrophic dysplasia; Pendrin; Prestin; Site-directed mutagenesis; Sulfate transporter; Transmembrane helix
dc.titleStructure and Function of a Model Member of the SulP Transporter Family
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume36
dc.date.issued2002
local.identifier.absfor060101 - Analytical Biochemistry
local.identifier.ariespublicationMigratedxPub23459
local.type.statusPublished Version
local.contributor.affiliationLoughlin, Patrick, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationShelden, Megan, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationTierney, Mary (Louise), College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHowitt, Susan, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue2-3
local.bibliographicCitation.startpage183
local.bibliographicCitation.lastpage190
local.identifier.doi10.1385/CBB:36:2-3:183
dc.date.updated2015-12-12T09:21:55Z
local.identifier.scopusID2-s2.0-0036362082
CollectionsANU Research Publications

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