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X-ray structure of ...
X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking.
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- Frick, Anna, 1982 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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- Kosinska-Eriksson, Urszula, 1976 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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de Mattia, Fabrizio (författare)
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- Öberg, Fredrik, 1982 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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- Hedfalk, Kristina, 1969 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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- Neutze, Richard, 1969 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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de Grip, Willem J (författare)
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Deen, Peter M T (författare)
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- Törnroth-Horsefield, Susanna, 1973 (författare)
- Lund University,Lunds universitet,Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- 2014-04-14
- 2014
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 1091-6490 .- 0027-8424. ; 111:17, s. 6305-10
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Abstract
Ämnesord
Stäng
- Human aquaporin 2 (AQP2) is a water channel found in the kidney collecting duct, where it plays a key role in concentrating urine. Water reabsorption is regulated by AQP2 trafficking between intracellular storage vesicles and the apical membrane. This process is tightly controlled by the pituitary hormone arginine vasopressin and defective trafficking results in nephrogenic diabetes insipidus (NDI). Here we present the X-ray structure of human AQP2 at 2.75 Å resolution. The C terminus of AQP2 displays multiple conformations with the C-terminal α-helix of one protomer interacting with the cytoplasmic surface of a symmetry-related AQP2 molecule, suggesting potential protein-protein interactions involved in cellular sorting of AQP2. Two Cd(2+)-ion binding sites are observed within the AQP2 tetramer, inducing a rearrangement of loop D, which facilitates this interaction. The locations of several NDI-causing mutations can be observed in the AQP2 structure, primarily situated within transmembrane domains and the majority of which cause misfolding and ER retention. These observations provide a framework for understanding why mutations in AQP2 cause NDI as well as structural insights into AQP2 interactions that may govern its trafficking.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- Aquaporin 2
- chemistry
- genetics
- metabolism
- Binding Sites
- Cadmium
- metabolism
- Calcium
- metabolism
- Crystallography
- X-Ray
- Diabetes Insipidus
- Nephrogenic
- metabolism
- Endoplasmic Reticulum
- metabolism
- Endosomal Sorting Complexes Required for Transport
- metabolism
- Humans
- Models
- Molecular
- Oocytes
- metabolism
- Protein Structure
- Secondary
- Protein Transport
- membrane protein
- X-ray crystallography
- water channel protein
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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Till lärosätets databas
- Av författaren/redakt...
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Frick, Anna, 198 ...
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Kosinska-Eriksso ...
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de Mattia, Fabri ...
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Öberg, Fredrik, ...
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Hedfalk, Kristin ...
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Neutze, Richard, ...
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visa fler...
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de Grip, Willem ...
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Deen, Peter M T
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Törnroth-Horsefi ...
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- Om ämnet
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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Proceedings of t ...
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Proceedings of t ...
- Av lärosätet
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Göteborgs universitet
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Lunds universitet