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α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats.

Hai A, Kizilbash NA - Bioinformation (2013)

Bottom Line: It is believed that unusual structural features permit A2-f to be targeted to the proximal tubule cell; to escape lysosomal degradation in liver and to enter the cytosol of proximal tubule cells of the kidneys.Homology modeling has been employed to determine the structural elements of this protein and they have been compared with the published structure of A2U.Results suggest differences between the structure of A2-f and its precursor protein A2U.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, Faculty of Medicine, Northern Border University, Arar-91431, Saudi Arabia.

ABSTRACT
The structure of α(2)-µ-Globulin fragment (A2-f) is not known.α(2)-µ-Globulin fragment (A2-f) is a 15.5 kDa protein that binds equimolar amount of fatty acids in male rat kidneys. The expression of this protein has been shown to change in response to druginduced and genetic hypertension which suggests that it plays an important role in renal fatty acid metabolism under pathological conditions as well as normal conditions. A2-f has sequence homology with amino acid 28-178 of α(2)-µ-Globulin (A2U) that is synthesized pre-dominantly in the male rat liver and is present in the urine. It is believed that unusual structural features permit A2-f to be targeted to the proximal tubule cell; to escape lysosomal degradation in liver and to enter the cytosol of proximal tubule cells of the kidneys. Homology modeling has been employed to determine the structural elements of this protein and they have been compared with the published structure of A2U. Results suggest differences between the structure of A2-f and its precursor protein A2U.

No MeSH data available.


Related in: MedlinePlus

Ribbon diagram of A2U based on the crystal structuresolved at 2.5 Å resolutions [18].
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Related In: Results  -  Collection


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Figure 4: Ribbon diagram of A2U based on the crystal structuresolved at 2.5 Å resolutions [18].


α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats.

Hai A, Kizilbash NA - Bioinformation (2013)

Ribbon diagram of A2U based on the crystal structuresolved at 2.5 Å resolutions [18].
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3569602&req=5

Figure 4: Ribbon diagram of A2U based on the crystal structuresolved at 2.5 Å resolutions [18].
Bottom Line: It is believed that unusual structural features permit A2-f to be targeted to the proximal tubule cell; to escape lysosomal degradation in liver and to enter the cytosol of proximal tubule cells of the kidneys.Homology modeling has been employed to determine the structural elements of this protein and they have been compared with the published structure of A2U.Results suggest differences between the structure of A2-f and its precursor protein A2U.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, Faculty of Medicine, Northern Border University, Arar-91431, Saudi Arabia.

ABSTRACT
The structure of α(2)-µ-Globulin fragment (A2-f) is not known.α(2)-µ-Globulin fragment (A2-f) is a 15.5 kDa protein that binds equimolar amount of fatty acids in male rat kidneys. The expression of this protein has been shown to change in response to druginduced and genetic hypertension which suggests that it plays an important role in renal fatty acid metabolism under pathological conditions as well as normal conditions. A2-f has sequence homology with amino acid 28-178 of α(2)-µ-Globulin (A2U) that is synthesized pre-dominantly in the male rat liver and is present in the urine. It is believed that unusual structural features permit A2-f to be targeted to the proximal tubule cell; to escape lysosomal degradation in liver and to enter the cytosol of proximal tubule cells of the kidneys. Homology modeling has been employed to determine the structural elements of this protein and they have been compared with the published structure of A2U. Results suggest differences between the structure of A2-f and its precursor protein A2U.

No MeSH data available.


Related in: MedlinePlus