1psl: Difference between revisions
New page: '''Theoretical Model''' The entry 1PSL is a Theoretical Model titled 'COMPUTATIONAL SEARCHING AND MUTAGENESIS SUGGEST A STRUCTURE FOR THE PENTAMERIC TRANSMEMBRANE DOMAIN OF PHOSPHOLAMBAN'... |
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{{Theoretical_model}} | |||
==COMPUTATIONAL SEARCHING AND MUTAGENESIS SUGGEST A STRUCTURE FOR THE PENTAMERIC TRANSMEMBRANE DOMAIN OF PHOSPHOLAMBAN== | |||
<StructureSection load='1psl' size='340' side='right'caption='[[1psl]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PSL FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1psl FirstGlance], [https://www.ebi.ac.uk/pdbsum/1psl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1psl ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structural and environmental constraints greatly simplify the folding problem for membrane proteins. Computational methods can be used in a global search to find a small number of chemically reasonable models within these constraints, such that a modest set of experimental data can distinguish among them. We show that, for phospholamban, the global search can be further simplified by reducing the problem to two-body, rather than many-body, interactions. This method of a constrained global search combined with experimental mutagenesis data yields a three-dimensional structure for this pentameric ion channel. The model is a left-handed symmetric homopentamer of alpha-helices with a well-defined channel, lined solely by hydrophobic residues. | |||
Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban.,Adams PD, Arkin IT, Engelman DM, Brunger AT Nat Struct Biol. 1995 Feb;2(2):154-62. PMID:7749920<ref>PMID:7749920</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1psl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Adams, P D]] | |||
[[Category: Arkin, I T]] | |||
[[Category: Brunger, A T]] | |||
[[Category: Engelman, D M]] | |||
Latest revision as of 12:34, 8 September 2021
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COMPUTATIONAL SEARCHING AND MUTAGENESIS SUGGEST A STRUCTURE FOR THE PENTAMERIC TRANSMEMBRANE DOMAIN OF PHOSPHOLAMBANCOMPUTATIONAL SEARCHING AND MUTAGENESIS SUGGEST A STRUCTURE FOR THE PENTAMERIC TRANSMEMBRANE DOMAIN OF PHOSPHOLAMBAN
Structural highlights
Publication Abstract from PubMedStructural and environmental constraints greatly simplify the folding problem for membrane proteins. Computational methods can be used in a global search to find a small number of chemically reasonable models within these constraints, such that a modest set of experimental data can distinguish among them. We show that, for phospholamban, the global search can be further simplified by reducing the problem to two-body, rather than many-body, interactions. This method of a constrained global search combined with experimental mutagenesis data yields a three-dimensional structure for this pentameric ion channel. The model is a left-handed symmetric homopentamer of alpha-helices with a well-defined channel, lined solely by hydrophobic residues. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban.,Adams PD, Arkin IT, Engelman DM, Brunger AT Nat Struct Biol. 1995 Feb;2(2):154-62. PMID:7749920[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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