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Folding of Aquapori...
Folding of Aquaporin 1 : Multiple evidence that helix 3 can shift out of the membrane core
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- Virkki, Minttu T. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab),Stockholm University, Solna, Sweden
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- Agrawal, Nitin (author)
- Åbo Akademi, Turku, Finland
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- Edsbäcker, Elin (author)
- Karolinska Institutet,Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab),Stockholm University, Solna, Sweden
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- Cristobal, Susana (author)
- Linköpings universitet,Avdelningen för cellbiologi,Hälsouniversitetet,University of the Basque Country, Leioa, Spain
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- Elofsson, Arne (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab),Stockholm University, Solna, Sweden
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- Kauko, Anni (author)
- Åbo Akademi, Turku, Finland
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(creator_code:org_t)
- 2014-05-14
- 2014
- English.
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In: Protein Science. - : Wiley. - 0961-8368 .- 1469-896X. ; 23:7, s. 981-992
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Abstract
Subject headings
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- The folding of most integral membrane proteins follows a two-step process: initially, individual transmembrane helices are inserted into the membrane by the Sec translocon. Thereafter, these helices fold to shape the final conformation of the protein. However, for some proteins, including Aquaporin 1 (AQP1), the folding appears to follow a more complicated path. AQP1 has been reported to first insert as a four-helical intermediate, where helix 2 and 4 are not inserted into the membrane. In a second step, this intermediate is folded into a six-helical topology. During this process, the orientation of the third helix is inverted. Here, we propose a mechanism for how this reorientation could be initiated: first, helix 3 slides out from the membrane core resulting in that the preceding loop enters the membrane. The final conformation could then be formed as helix 2, 3, and 4 are inserted into the membrane and the reentrant regions come together. We find support for the first step in this process by showing that the loop preceding helix 3 can insert into the membrane. Further, hydrophobicity curves, experimentally measured insertion efficiencies and MD-simulations suggest that the barrier between these two hydrophobic regions is relatively low, supporting the idea that helix 3 can slide out of the membrane core, initiating the rearrangement process.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- membrane protein
- translocon recognition
- protein folding
- hydrophobicity
- molecular dynamics
Publication and Content Type
- ref (subject category)
- art (subject category)
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