Interleukin-1 beta: Difference between revisions

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'''THREE-DIMENSIONAL STRUCTURE OF IL-1β'''

The molecule contains 12 antiparallel β-strands. The molecule has internal pseudo threefold symmetry with the molecule representing a conical barrel with a shallow open face on one end and a closed face on the other. The amino and carboxy termini are ~~close to each other~~ at the "open end" of the barrel~~. Two of the five 1-hairpins in this molecule~~ are ~~located in the "open end" and three at the "closed end"~~. 24 hydrophobic side chains ~~line~~ the inner surface of the barrel and both the ends of the barrel ~~have concentrations of exposed polar residues~~. More detail structure information could be found in reference[4].

The molecule contains 12 antiparallel β-strands. The molecule has internal pseudo threefold symmetry with the molecule representing a conical barrel with a shallow open face on one end and a closed face on the other. The amino and carboxy termini are located at the "open end" of the barrel and they are close to each other. 24 hydrophobic side chains are present in the inner surface of the barrel and polar residues are found to be exposed on both the ends of the barrel. More detail structure information could be found in reference[4].

<scene name='57/571319/Scene1/1'>Human Interleukin-1 beta</scene> are present in the 3D structure. In the picture we could see <scene name='57/571319/Scene1/2'>helix</scene> was colored as purple and <scene name='57/571319/Scene1/2'>sheet</scene> was colored as blue, respectively. Most <scene name='57/571319/Scene1/3'>conserved area</scene> ,which is dark red color, was buried inside of the protein.

Interleukin-1 beta: Difference between revisions

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@@ Line 8: / Line 8: @@
 '''THREE-DIMENSIONAL STRUCTURE OF IL-1β'''
-The molecule contains 12 antiparallel β-strands. The molecule has internal pseudo threefold symmetry with the molecule representing a conical barrel with a shallow open face on one end and a closed face on the other. The amino and carboxy termini are close to each other at the "open end" of the barrel. Two of the five 1-hairpins in this molecule are located in the "open end" and three at the "closed end". 24 hydrophobic side chains line the inner surface of the barrel and both the ends of the barrel have concentrations of exposed polar residues. More detail structure information could be found in reference[4].
+The molecule contains 12 antiparallel β-strands. The molecule has internal pseudo threefold symmetry with the molecule representing a conical barrel with a shallow open face on one end and a closed face on the other. The amino and carboxy termini are located at the "open end" of the barrel and they are close to each other. 24 hydrophobic side chains are present in the inner surface of the barrel and polar residues are found to be exposed on both the ends of the barrel. More detail structure information could be found in reference[4].
 <scene name='57/571319/Scene1/1'>Human Interleukin-1 beta</scene> are present in the 3D structure. In the picture we could see <scene name='57/571319/Scene1/2'>helix</scene> was colored as purple and <scene name='57/571319/Scene1/2'>sheet</scene> was colored as blue, respectively. Most <scene name='57/571319/Scene1/3'>conserved area</scene> ,which is dark red color, was buried inside of the protein.