دورية أكاديمية
أعرض في EDS

Inverted topologies in membrane proteins: a mini-review.

التفاصيل البيبلوغرافية
العنوان: Inverted topologies in membrane proteins: a mini-review.
المؤلفون: Duran AM; Center for Structural Biology, Department of Chemistry, Vanderbilt University, Nashville, TN 37212, USA., Meiler J; Center for Structural Biology, Department of Chemistry, Vanderbilt University, Nashville, TN 37212, USA.
المصدر: Computational and structural biotechnology journal [Comput Struct Biotechnol J] 2013 Nov 09; Vol. 8, pp. e201308004. Date of Electronic Publication: 2013 Nov 09 (Print Publication: 2013).
نوع المنشور: Journal Article; Review
اللغة: English
بيانات الدورية: Publisher: Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology Country of Publication: Netherlands NLM ID: 101585369 Publication Model: eCollection Cited Medium: Print ISSN: 2001-0370 (Print) Linking ISSN: 20010370 NLM ISO Abbreviation: Comput Struct Biotechnol J Subsets: PubMed not MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology
Original Publication: Gothenburg, Sweden : Research Network of Computational and Structural Biotechnology
مستخلص: Helical membrane proteins such as transporters, receptors, or channels often exhibit structural symmetry. Symmetry is perfect in homo-oligomers consisting of two or more copies of the same protein chain. Intriguingly, in single chain membrane proteins, often internal pseudo-symmetry is observed, in particular in transporters and channels. In several cases single chain proteins with pseudo-symmetry exist, that share the fold with homo-oligomers suggesting evolutionary pathways that involve gene duplication and fusion. It has been hypothesized that such evolutionary pathways allow for the rapid development of large proteins with novel functionality. At the same time symmetry can be leveraged to recognize highly symmetric substrates such as ions. Here we review helical transporter proteins with an inverted two-fold pseudo-symmetry. In this special scenario the symmetry axis lies in the membrane plane. As a result, the putative ancestral monomeric protein would insert in both directions into the membrane and its open-to-the-inside and open-to-the-outside conformations would be structurally identical and iso-energetic, giving a possible evolutionary pathway to create a transporter protein that needs to flip between the two states.
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معلومات مُعتمدة: R01 DK097376 United States DK NIDDK NIH HHS; R01 GM080403 United States GM NIGMS NIH HHS; R01 GM099842 United States GM NIGMS NIH HHS; R01 MH090192 United States MH NIMH NIH HHS
فهرسة مساهمة: Keywords: Membrane protein; gene duplication; gene fusion; inverted topology; pseudo-symmetry; symmetry
تواريخ الأحداث: Date Created: 20140402 Date Completed: 20140624 Latest Revision: 20211021
رمز التحديث: 20240829
مُعرف محوري في PubMed: PMC3962082
DOI: 10.5936/csbj.201308004
PMID: 24688744
قاعدة البيانات: MEDLINE
الوصف
تدمد:2001-0370
DOI:10.5936/csbj.201308004