User:Chengfeng Ren/IFN beta 1a: Difference between revisions

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Interferon-β has two subtyes, interferon-β-1a and interferon-β-1b. Interferon-β-1a is naturally expressed in numerous cell types in human, including

fibroblasts, endothelial cells, epithelial cells and various leukocytes, however,Interferon-β-1b is produced in modified E. coli.

~~Interferon-β-1a tends to aggregate and form dimers.<scene name='56/566503/Interferon_dimer/1'>Interferon dimer</scene>~~

Here is a jpg clearly illustrating IFNs categories.

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=='''Structure info. of IFNβ-1a'''==

IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a <scene name='56/566503/Disulfide_bridge/1'>disulfide bridge</scene> with Cys-141 of and plays an important role in the stabilization of protein structure

IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a <scene name='56/566503/Disulfide_bridge/1'>disulfide bridge</scene> with Cys-141 of and plays an important role in the stabilization of protein structure.

Interferon-β-1a tends to aggregate and form dimers.<scene name='56/566503/Interferon_dimer/1'>Interferon dimer</scene>

A zinc ion is observed to exist at the interface between chains A and B. It is coordinated in a tetrahedral manner by His-121 of molecule A and His-93 and His-97 of molecule B. A water molecule occupies the fourth coordination site. A network of hydrogen bonds formed between His-121 and Glu-43 (molecule A) and between His-97 and Gln-94 (molecule B) appears to assist in the stabilization of the zinc-binding site.

<scene name='56/566498/Interferon_beta_1a/1'>Interferon beta 1a</scene>

@@ Line 17: / Line 17: @@
 Interferon-β has two subtyes, interferon-β-1a and interferon-β-1b. Interferon-β-1a is naturally expressed in numerous cell types in human, including
 fibroblasts, endothelial cells, epithelial cells and various leukocytes, however,Interferon-β-1b is produced in modified E. coli.
-Interferon-β-1a tends to aggregate and form dimers.<scene name='56/566503/Interferon_dimer/1'>Interferon dimer</scene>
 Here is a jpg clearly illustrating IFNs categories.
@@ Line 23: / Line 22: @@
 =='''Structure info. of IFNβ-1a'''==
-IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a <scene name='56/566503/Disulfide_bridge/1'>disulfide bridge</scene> with Cys-141 of and plays an important role in the stabilization of protein structure
+IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a <scene name='56/566503/Disulfide_bridge/1'>disulfide bridge</scene> with Cys-141 of and plays an important role in the stabilization of protein structure.
+Interferon-β-1a tends to aggregate and form dimers.<scene name='56/566503/Interferon_dimer/1'>Interferon dimer</scene>
+A zinc ion is observed to exist at the interface between chains A and B. It is coordinated in a tetrahedral manner by His-121 of molecule A and His-93 and His-97 of molecule B. A water molecule occupies the fourth coordination site. A network of hydrogen bonds formed between His-121 and Glu-43 (molecule A) and between His-97 and Gln-94 (molecule B) appears to assist in the stabilization of the zinc-binding site.
 <scene name='56/566498/Interferon_beta_1a/1'>Interferon beta 1a</scene>