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| - | Proposed Title: <span style="font-size:150%">'''Nitrotyrosine.'''</span>
| + | <font color="red">Please do not edit this page. Thank you, [[User:Eric Martz]], June 2011.</font> |
| - | <center><table cellpadding="8" border="1" width="90%" style="background: #ffe0b0;"><tr><td>
| + | <Structure load='1d66' size='450' frame='true' align='right' caption='Insert caption here' scene='Sandbox7_Eric_Martz/Test1/1' /> |
| - | This page is reserved for a collaboration between [[User:Eric Martz]] and [http://www.cancer.ucla.edu/index.aspx?page=645&recordid=338 Hermes J Garbán].
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| - | </td></tr></table></center> | + | |
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| - | [[Image:800px-Nitrotyrosine.png|right|thumb|3-Nitrotyrosine]]
| + | <scene name='Sandbox7_Eric_Martz/Test1/1'>TextToBeDisplayed</scene> |
| - | Nitrotyrosine results from the post-translational modification of the [[Standard Residues|standard amino acid]] tyrosine. Reactive nitrogen compounds produced in inflammation are typically responsible. Nitrosylation of tyrosine tends to inactivate enzymes. In March, 2011, there are 13 entries in the [[PDB]] containing coordinates for 3-nitrotyrosine (meta-nitro-tyrosine), with the [[http://www.proteopedia.org/wiki/index.php/Non-Standard_Residues|compound ID]] '''NIY'''. These include six sequence-distinct proteins, represented by ribonucleotide reductase [[2xof]] and [[2xap]], laccase [[3div]], Human Manganese Superoxide Dismutase [[2adp]], Human Glutathione Reductase [[1k4q]], and bovine Cu,Zn superoxide dismutase [[1sda]]. Not surprisingly, the NO<sub>2</sub> adduct, being very hydrophilic, is often on the surface of the protein.
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| - | {{Clear}}
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| - | <Structure size='450' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here'
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| - | scene='Sandbox7_Eric_Martz/Cartoon/1' />
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| - | One of the more interesting cases may be Human <font color="#00c000">'''Manganese'''</font> Superoxide Dismutase, for which structures are available for the wild type [[2adq]], shown at right (<scene name='Sandbox7_Eric_Martz/Cartoon/1'>restore initial scene</scene>), and the nitrated form, [[2adp]]. In this structure, <font color="#00c000">'''Mn<sup>++</sup>'''</font> is <scene name='Sandbox7_Eric_Martz/Cartoon/2'>buried</scene>. The is
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| - | <scene name='Sandbox7_Eric_Martz/Mn_contacts/1'>caged</scene> by four histidine <font color="#3050F8">'''nitrogens'''</font>, one aspartate <font color="#ff0d0d">'''oxygen'''</font>, and one <font color="magenta">'''water'''</font>. Tyrosine 34 is nearby (5.2 Ångstroms), but not near enough to be interacting with the <font color="#00c000">'''Mn<sup>++</sup>'''</font> or its cage.
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| - | <scene name='Sandbox7_Eric_Martz/Contacts_to_nitrotyrosine/1'>Nitrosylation of tyrosine 34</scene> extends it towards the <font color="#00c000">'''Mn<sup>++</sup>'''</font>. The partially negatively charged <font color="#ff0d0d">'''oxygens'''</font> in the NO<sub>2</sub> are 3.6-3.8 Å from the electron-hungry <font color="#00c000">'''Mn<sup>++</sup>'''</font>. <scene name='Sandbox7_Eric_Martz/Aligned_pre_and_post_nitro/2'>Nitrosylation pushes the tyrosine ring</scene> slightly farther from the <font color="#00c000">'''Mn<sup>++</sup>'''</font>, but causes no other significant conformational changes<ref>[[DeepView]] was used to align all atoms of the three Mn-coordinating histidines. In the resulting file [[Image:2adq-2adp-3hisaln.pdb]], 2adq is model 1, and 2adp is model 2.</ref>.
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| | + | <scene name='Sandbox7_Eric_Martz/Test/1'>color key test from Test Acct 2</scene> |
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| | + | <scene name='Sandbox7_Eric_Martz/Test/2'>color key from EM</scene> |
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| - | ==See Also==
| + | Scenes made in Apple OS 10.7 Lion |
| - | * [http://en.wikipedia.org/wiki/Nitrotyrosine Nitrotyrosine] in Wikipedia. | + | *<scene name='Sandbox7_Eric_Martz/Test2/2'>TextToBeDisplayed</scene> |
| | + | *<scene name='Sandbox7_Eric_Martz/Test2/3'>TextToBeDisplayed</scene> |
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| - | ==Notes==
| + | (available) |
| - | <references />
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