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Comparative structural analysis of lipid binding START domains

Thorsell, Ann-Gerd ; Lee, Wen Hwa ; Persson, Camilla ; Siponen, Marina I ; Nilsson, Martina ; Busam, Robert D ; Kotenyova, Tetyana ; Schüler, Herwig LU orcid and Lehtiö, Lari (2011) In PLoS ONE 6(6).
Abstract

BACKGROUND: Steroidogenic acute regulatory (StAR) protein related lipid transfer (START) domains are small globular modules that form a cavity where lipids and lipid hormones bind. These domains can transport ligands to facilitate lipid exchange between biological membranes, and they have been postulated to modulate the activity of other domains of the protein in response to ligand binding. More than a dozen human genes encode START domains, and several of them are implicated in a disease.

PRINCIPAL FINDINGS: We report crystal structures of the human STARD1, STARD5, STARD13 and STARD14 lipid transfer domains. These represent four of the six functional classes of START domains.

SIGNIFICANCE: Sequence alignments based on these... (More)

BACKGROUND: Steroidogenic acute regulatory (StAR) protein related lipid transfer (START) domains are small globular modules that form a cavity where lipids and lipid hormones bind. These domains can transport ligands to facilitate lipid exchange between biological membranes, and they have been postulated to modulate the activity of other domains of the protein in response to ligand binding. More than a dozen human genes encode START domains, and several of them are implicated in a disease.

PRINCIPAL FINDINGS: We report crystal structures of the human STARD1, STARD5, STARD13 and STARD14 lipid transfer domains. These represent four of the six functional classes of START domains.

SIGNIFICANCE: Sequence alignments based on these and previously reported crystal structures define the structural determinants of human START domains, both those related to structural framework and those involved in ligand specificity.

ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.

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author
; ; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Adaptor Proteins, Vesicular Transport, Carrier Proteins/chemistry, Crystallography, X-Ray/methods, GTPase-Activating Proteins, Humans, Palmitoyl-CoA Hydrolase/chemistry, Phosphoproteins/chemistry, Tumor Suppressor Proteins/chemistry
in
PLoS ONE
volume
6
issue
6
article number
e19521
publisher
Public Library of Science (PLoS)
external identifiers
  • pmid:21738568
  • scopus:79959701884
ISSN
1932-6203
DOI
10.1371/journal.pone.0019521
language
English
LU publication?
no
id
525220f8-ad14-4dd8-bf18-68e3498d3566
date added to LUP
2024-11-21 17:59:45
date last changed
2025-05-23 19:59:20
@article{525220f8-ad14-4dd8-bf18-68e3498d3566,
  abstract     = {{<p>BACKGROUND: Steroidogenic acute regulatory (StAR) protein related lipid transfer (START) domains are small globular modules that form a cavity where lipids and lipid hormones bind. These domains can transport ligands to facilitate lipid exchange between biological membranes, and they have been postulated to modulate the activity of other domains of the protein in response to ligand binding. More than a dozen human genes encode START domains, and several of them are implicated in a disease.</p><p>PRINCIPAL FINDINGS: We report crystal structures of the human STARD1, STARD5, STARD13 and STARD14 lipid transfer domains. These represent four of the six functional classes of START domains.</p><p>SIGNIFICANCE: Sequence alignments based on these and previously reported crystal structures define the structural determinants of human START domains, both those related to structural framework and those involved in ligand specificity.</p><p>ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.</p>}},
  author       = {{Thorsell, Ann-Gerd and Lee, Wen Hwa and Persson, Camilla and Siponen, Marina I and Nilsson, Martina and Busam, Robert D and Kotenyova, Tetyana and Schüler, Herwig and Lehtiö, Lari}},
  issn         = {{1932-6203}},
  keywords     = {{Adaptor Proteins, Vesicular Transport; Carrier Proteins/chemistry; Crystallography, X-Ray/methods; GTPase-Activating Proteins; Humans; Palmitoyl-CoA Hydrolase/chemistry; Phosphoproteins/chemistry; Tumor Suppressor Proteins/chemistry}},
  language     = {{eng}},
  number       = {{6}},
  publisher    = {{Public Library of Science (PLoS)}},
  series       = {{PLoS ONE}},
  title        = {{Comparative structural analysis of lipid binding START domains}},
  url          = {{http://dx.doi.org/10.1371/journal.pone.0019521}},
  doi          = {{10.1371/journal.pone.0019521}},
  volume       = {{6}},
  year         = {{2011}},
}