Template:Team:Bonn:NetworkData

content.titleShort = "Direct inhibition and activation";

content.titleShort = "Direct inhibition and activation";

content.titleLong = "Direct inhibition and activation";

content.titleLong = "Direct inhibition and activation";

content.text= "Moreover proteins can be regulated directly in many different ways. Binding of other Proteins or small molecules for example can activate or deactivate the catalytic function of proteins. For example small molecules can have great impact on protein function. They can often influence protein functions by binding to an allosteric center. Small molecules can be activating, as well as repressing, depending on the type of the molecule^{<a href=#11.1>11.1</a>}.</br></br><div class='content-image'> <img src='https://static.igem.org/mediawiki/2013/1/1c/BonnSmallMolecules.jpg' width='550'> </br>Different mechanisms for small-molecule activation of enzymes^{<a href=#11.2>11.2</a>} </div></br></br>The following picture shows the example of the allosteric activation of a glucokinase</br> <div class='content-image'> <img src=https://static.igem.org/mediawiki/2013/f/f4/BonnSmallMolecules2.jpg></br>&quot;(a) GK bound to the GKA, compound A, and glucose (blue, Protein Data Bank (PDB) ID 1V4S). Compound A binds at a site distal from the active site, which is highlighted by the presence of the substrate, glucose. (b) Structural overlay of GK in the presence of compound A and glucose with an unliganded, inactive GK (pink, PDB ID 1V4T). In the unbound GK, the GKA binding site is occluded. A large shift in the small subunit of GK occurs from the unbound to bound structures (black arrow). Glucose promotes the active conformation, which is hindered from shifting back to the inactive conformation in the presence of compound A. (c) 7 mutations (out of 13)9 identified in GK (pink) that are associated with disease map to the GKA binding site. These mutations highlight an important regulatory site within GK, and could similarly stabilize a closed, active conformation.&quot;^{<a href=#11.2>[11.2]</a>}</div></br></br><p><a name=11.1>11.1</a><a href='http://www.nature.com/nrd/journal/v3/n4/full/nrd1343.html'>Small-molecule inhibitors of protein–protein interactions: progressing towards the dream; Michelle R. Arkin & James A. Wells</a>/p></br><p><a name=11.2>11.2</a><a href='http://www.nature.com/nchembio/journal/v6/n3/full/nchembio.318.html'>Turning enzymes ON with small molecules, Julie A Zorn & James A Wells</a></p>";

content.text= "Moreover proteins can be regulated directly in many different ways. Binding of other Proteins or small molecules for example can activate or deactivate the catalytic function of proteins. For example small molecules can have great impact on protein function. They can often influence protein functions by binding to an allosteric center. Small molecules can be activating, as well as repressing, depending on the type of the molecule^{<a href=#11.1>11.1</a>}.</br></br><div class='content-image'> <img src='https://static.igem.org/mediawiki/2013/1/1c/BonnSmallMolecules.jpg' width='550'> </br>Different mechanisms for small-molecule activation of enzymes^{<a href=#11.2>11.2</a>} </div></br></br>The following picture shows the example of the allosteric activation of a glucokinase</br> <div class='content-image'> <img src=https://static.igem.org/mediawiki/2013/f/f4/BonnSmallMolecules2.jpg></br>&quot;(a) GK bound to the GKA, compound A, and glucose (blue, Protein Data Bank (PDB) ID 1V4S). Compound A binds at a site distal from the active site, which is highlighted by the presence of the substrate, glucose. (b) Structural overlay of GK in the presence of compound A and glucose with an unliganded, inactive GK (pink, PDB ID 1V4T). In the unbound GK, the GKA binding site is occluded. A large shift in the small subunit of GK occurs from the unbound to bound structures (black arrow). Glucose promotes the active conformation, which is hindered from shifting back to the inactive conformation in the presence of compound A. (c) 7 mutations (out of 13)9 identified in GK (pink) that are associated with disease map to the GKA binding site. These mutations highlight an important regulatory site within GK, and could similarly stabilize a closed, active conformation.&quot;^{<a href=#11.2>[11.2]</a>}</div></br></br><p><a name=11.1>11.1</a><a href='http://www.nature.com/nrd/journal/v3/n4/full/nrd1343.html'>Small-molecule inhibitors of protein–protein interactions: progressing towards the dream; Michelle R. Arkin & James A. Wells</a>/p></br><p><a name=11.2>11.2</a><a href='http://www.nature.com/nchembio/journal/v6/n3/full/nchembio.318.html'>Turning enzymes ON with small molecules, Julie A Zorn & James A Wells</a></p>";

content.type="Background";

content.type="Background";