Sandbox WWC4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
<StructureSection load='1h6i' size='350' side='right' caption='Aquaporin' scene='Aquaporin with ligand'>
<StructureSection load='1h6i' size='350' side='right' caption='Aquaporin' scene='Aquaporin with ligand'>
-
Aquqporin (AQP) is a integral membrane proteins that control the amount of water that travels in and out of the cell<ref name="Takata">PMID:15242101</ref>. Before the discovery of aquaporin by Peter Agre (1992); it was thought that water molecules leaked through the phospholipid bilayer one by one. However this could not be the case for cells that released and uptake water such as in the kidneys.
+
Aquqporin (AQP) is a integral membrane proteins that control the amount of water that travels in and out of the cell<ref name="Takata">PMID:15242101</ref>. Before the discovery of aquaporin by Peter Agre (1992); it was thought that water molecules leaked through the phospholipid bilayer one by one. However this could not be the case for cells that need to released and uptake water like in the kidneys.
Aquaporins allow water to flow rapidly to the inside of cell then it would by crossing the bilayer.<ref name="Takata" />
Aquaporins allow water to flow rapidly to the inside of cell then it would by crossing the bilayer.<ref name="Takata" />
-
This protein is highly selective to water molecules , preventing the passage of ions and other solutes.There are multiple types of aquaporins that can allow the transport of other molecules such as glycerol,CO2, ammonia and urea by aquaglyceroporin. It depends on the size of the pore; aquaporin 3 channel has a pore width of 8-10 Ångströms and allows the passage of hydrophilic molecules ranging between 150-200 Da<ref name="Takata" />. Aquaporins water channel are impermeable to protons and other charged species
+
This protein is highly selective to water molecules , preventing the passage of ions and other solutes.There are multiple types of aquaporins that can allow the transport of other molecules such as glycerol,CO2, ammonia and urea. Aquaporin 3 has a pore width of 8-10 Ångströms and allows the passage of hydrophilic molecules ranging between 150-200 Da<ref name="Takata" />. Aquaporins water channel are impermeable to protons and other charged species.
Water molecules traverse through the pore of the channel in single file<ref name="Takata" />. The presence of water channels increases membrane permeability to water<ref name="Takata" />.
Water molecules traverse through the pore of the channel in single file<ref name="Takata" />. The presence of water channels increases membrane permeability to water<ref name="Takata" />.
'''Structure'''
'''Structure'''
-
Aquaporin is protien with six transmembrane alpha helices with the amino and craboxyl terminal located in the cytoplasm.<ref name="Murata">PMID:11034202</ref>
+
Aquaporin is a protien with six transmembrane alpha helices with the amino and craboxyl terminal tails located in the cytoplasm.<ref name="Murata">PMID:11034202</ref>. Each monomer is able to channel water.There is a conserved Asn-Pro-Ala sequence that overlap in the middle of the lipid bilayer membrane which creates the'hourglass' structure of the aquaporin. The hourglass shape allows the water flows, these water pores are completely impermeable to charged species, such as protons. Which is very important to the conservation of membrane's electrochemical potential<ref name="Takata" />.
-
Each monomer is able to channel water.There is a conserved Asn-Pro-Ala sequence that overlap in the middle of the lipid bilayer membrane which creates the'hourglass' structure of the aquaporin.The hourglass shape allows the water flows, these water pores are completely impermeable to charged species, such as protons. Which is very important to the conservation of membrane's electrochemical potential<ref name="Takata" />.
+
<scene name='69/696849/Chains_of_aquaporin/1'>Chains of Aquaporin (Click to View)</scene>
<scene name='69/696849/Chains_of_aquaporin/1'>Chains of Aquaporin (Click to View)</scene>
Line 33: Line 32:
'''Function'''
'''Function'''
-
There are thirteen known types of aquaporins in mammals, and six of these are located in the kidney. The most studied aquaporins are AQP1, AQP2, AQP3, and AQP4.The location of Aquaporin is usually found in the kidney, eye in the body. <ref name="Cardiac"> PMID: 24158693 </ref>
+
There are thirteen known types of aquaporins in mammals, and six of these are located in the kidney. The most studied aquaporins are AQP1, AQP2, AQP3, and AQP4. The location of Aquaporin is usually found in the kidney, eye in the body. <ref name="Cardiac"> PMID: 24158693 </ref>
In the Kidney, they are found in the basolateral and apical plasma membranes of the proximal tubules and the limb of the loop of Henle in the kidney.Aquaporin are concentrated in the kidney is where there is a need to transporting large amounts of water in and out of the cell.<ref name="Cardiac" />
In the Kidney, they are found in the basolateral and apical plasma membranes of the proximal tubules and the limb of the loop of Henle in the kidney.Aquaporin are concentrated in the kidney is where there is a need to transporting large amounts of water in and out of the cell.<ref name="Cardiac" />
Line 39: Line 38:
[[Image:F2.large.jpg|300px|left|thumb|Water Orientation in AQP]]
[[Image:F2.large.jpg|300px|left|thumb|Water Orientation in AQP]]
-
Aquqporin was also found in the plants.
 
- 
-
If a person is identified with severe or total deficiency in aquaporin-1. They are generally healthy, they might have a disorder that cause an increase in urine production.<ref name="Cardiac" />
 
Additionally, it is found in red blood cells, vascular endothelium, the gastrointestinal tract, sweat glands, and lungs.
Additionally, it is found in red blood cells, vascular endothelium, the gastrointestinal tract, sweat glands, and lungs.
 +
 +

Revision as of 05:15, 14 May 2015

Aquaporin (AQP) The Water Channel of the cell

Aquaporin

Drag the structure with the mouse to rotate
Personal tools