Ann Taylor sandbox 10

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(New page: <applet load="1ppb" size="350" color="white" frame="true" align="left" spinBox="true" caption="Human Thrombin with PPACK inhibitor" /> '''Serine proteases''', or '''proteinases''', so ca...)
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<applet load="1ppb" size="350" color="white" frame="true" align="left" spinBox="true"
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== Your Heading Here (maybe something like 'Structure') ==
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caption="Human Thrombin with PPACK inhibitor" />
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<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
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Anything in this section will appear adjacent to the 3D structure and will be scrollable.
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'''Serine proteases''', or '''proteinases''', so called due to the presence of a serine residue in the active site, are a class of enzymes that catalyse the hydrolysis of peptide bonds in proteins.
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This sandbox is for use by a BCMB 402 student.
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==Thrombin==
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</StructureSection>
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'''Thrombin''' is a "trypsin-like" serine protease. Its structure (PDB code [[1ppb]]) is shown here with a peptide chloroketone inhibitor (PPACK). The thrombin A chain (cleaved N terminal fragement) is shown in cyan and the B chain is shown in red. The <scene name='Serine_Protease/Active_site/2'>Active site</scene> is made up of a catalytic triad of Ser195, His57 and Asp102, backed up by Ser214. The peptide chloroketone inhibitor (PPACK) is shown in purple. A closeup shows the <scene name='Serine_Protease/Activation_site/2'>activation site</scene> at which the sidechain of Asp194 makes a salt link with the N-terminus at residue 16, newly formed when the A chain is cleaved in the zymogen-to-enzyme activation process. The specificity pocket is on one side of the throat of the domain 2 beta barrel, and the activation site is close next to it.
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The B chain consists of <scene name='Serine_Protease/Domains/1'>two domains</scene>. As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel. The specificity pocket (here filled with the Lys sidechain of the PPACK inhibitor) is in one side of the throat of the domain 2beta barrel, and the activation site is close next to it.
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<applet load="2ptc" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="Trypsin BPT1 complex" />
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==Trypsin-BPTI complex==
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The trypsin backbone is shown in pink and the trypsin inhibitor, BPTI, in yellow (PDB code [[2ptc]]). The <scene name='Serine_Protease/Active_site/3'>active site</scene> residues [Ser195-His57-Asp102-Ser214] are shown in green, the disulfide bond between residues 14-38 is shown in yellow and the Lys 15 sidechain at the specificity site in pink.
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{{Clear}}
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== '''Content Donators''' ==
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* Content for this page has been included and adapted with permission from Jane S. and David C. Richardson's http://kinemage.biochem.duke.edu/
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Revision as of 17:57, 26 September 2013

Your Heading Here (maybe something like 'Structure')

Structure of HMG-CoA reductase (PDB entry 1dq8)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Melissa Kramer, Ann Taylor

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