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| <div style="font-size:175%; padding-top:0.5em; padding-left:30.0px;">Welcome to Proteopedia,</div> | |
| <div style="border:0px; padding:0px; margin=0px; line-height:2.0em; padding-left:30.0px;">The free, collaborative 3D encyclopedia of proteins & other molecules</div>
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| <td align="left" width="50%">[[Proteopedia:About|About]] <font color="blue">•</font> [[Help:Editing|Editing]] <font color="blue">•</font> [[Help:Contents|Help]]</td>
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| <td align="right" width="50%">[[Proteopedia:Video_Guide|Video Guide]] <font color="blue">•</font> [[Proteopedia:Interesting_Pages|Content (Topic Pages)]] <font color="blue">•</font> [[Proteopedia:What%27s_New|What's New]]</td>
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| <table style="background: #D1FFE7; border:1px solid #94FFC8" cellspacing="5px" cellpadding="10px">
| | H274Y ([[Amino Acids#Histidine|Histidine]] to [[Amino Acids#Tyrosine|Tyrosine]]) is the most common mutation conferring resistance to the drug Tamiflu in the neuraminidase N1 of Influenza A (e.g. H1N1, H5N1). Although resistant, this mutant N1 still binds Tamiflu weakly, and a crystal structure was obtained, [[3ckz]]. Below, this is compared to the wild type, [[2hu4]]], using structural alignment of a single protein chain:Tamiflu complex from each. |
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| <div style="font-size:120%" align="left">Currently featured article</div>
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| <applet load='2q66' size='300' frame='false' scene='Proteopedia:Main_page_develop/2q66_initial/3' />
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| <div style="font-size:130%; line-height:2.0em"><span style="color:green" align="center">Green</span> links change the 3D image!</div>
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| <div style="font-size:200%; line-height:2.0em">[[2q66]] - Poly(A) polymerase</div>
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| Poly(A) polymerase binds specifically to ATP and adds it the end of a mRNA chain. This structure contains an oligo(A) polynucleotide with 5 nucleotides, an ATP molecule, and a magnesium ion. … In the <scene name='2q66/2q66_summary/1'>3D figure</scene>, the enzyme is shown as a blue backbone, the RNA chain in yellow, the ATP in red, the Mg<sup>++</sup> in green, and ALA154 in magenta. Several mechanisms are used to achieve the specificity for ATP. The Mg<sup>++</sup> is coordinated by <scene name='2q66/2q66_asp/2'>ASP100 and ASP102</scene>, and the Mg<sup>++</sup> coordinates with the phosphates of ATP, positioning the nucleotide in the active site. The adenine base is sandwiched between the <scene name='2q66/2q66_stacking/2'>terminal base of the RNA (in yellow) and VAL234 (in cyan)</scene>. [[2q66|Read more...]]
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| ----
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| <table style="background: #D1FFE7; border:1px solid #94FFC8" cellspacing="5px" cellpadding="10px" width="100%">
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| <div style="font-size:120%" align="left">Browse</div>
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| <div style="font-size:120%; line-height:2.0em">Favorites</div>
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| <div style="font-size:120%; line-height:2.0em">Find my protein/molecule</div>
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| <div style="font-size:120%; line-height:2.0em">'''What's new?'''</div>
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| * [[Hemoglobin]] - the protein in your blood responsible for oxygen transport
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| * [[HIV-1 protease]] - a protein made by the HIV virus, crucial for infection
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| * [[Lac repressor]] - controls expression of bacterial enzymes involved in lactose metabolism
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| <div align="right">[[Favorites|More]]...</div>
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| * All [[PDB]] entries (over 57,000) have pages
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| * ''Go'' takes you directly to the page if it exists,
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| * ''Search'' gives you search results
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| <div align="right">[[Help:Searching|More]]...</div>
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| <td width="33%" valign="top">
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| * Mini-biography on [[Frederic M. Richards]], an eminent protein structure and function researcher
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| * [[Mechanosensitive_channels:_opening_and_closing]] - channels involved in touch, hearing, and in maintaining osmotic balance
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| * [[1e08]], an iron-iron hydrogenase transferring its electrons to a cytochrome
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| <div align="right">[[Proteopedia:What%27s_New| More]]...</div>
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| | '''Why is the affinity of Tamiflu reduced by the mutation H274Y?''' Use the scenes below to help answer this question. |
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| | Tamiflu is shown as thick sticks. Atoms contacting Tamiflu (4 Å) are shown as balls. Amino acids that contain contacting atoms, plus amino acid 274, are shown as thin sticks. All other amino acids are hidden. |
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| <div style="font-size:120%" align="left">Want to contribute?</div>
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| <div align="center">Pages are easy to create and edit, and <font color='green'>'''Green links'''</font> are easy to make! </div>
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| <div style="font-size:120%; line-height:2.0em">Step 1</div>
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| <div style="font-size:120%; line-height:2.0em">Step 2</div>
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| <div style="font-size:120%; line-height:2.0em">Step 3</div>
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| [[Special:RequestAccount|Request an account]].<br/>''(Members of the scientific community, including students and educators.)''
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| <td width="34%" valign="top">
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| Get started with our narrated [[Proteopedia:Video_Guide|video guide]], then use our [[Help:Editing|editing-help page]] as a reference.
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| Help expand existing pages like [[1twc]] or [[Prion proteins]]; or [[Help:Editing#How_To_Create_A_New_Page|start a new page]] on your favorite topic. We could use pages on [[DNA]], [[Trypsin]], & [[Myoglobin]], among [[Wanted pages|others]].
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| ''(Consider joining the [[Proteopedia:Page of the Year Competition| Page of the Year Competition]] to win an iPod Touch.)''
| | Influenza neuraminidase N1: |
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| ----
| | <jmol> |
| <table style="background: #D1FFE7; border:1px solid #94FFC8" cellspacing="5px" cellpadding="10px" width="100%"> | | <jmolButton> |
| <tr> | | <script>anim off; frame 1.2</script> |
| <th style="background: #94FFC8;" width ="100%" colspan="3"> | | <text>H274Y</text> |
| <div style="font-size:120%" align="left">What can Proteopedia do for me?</div> | | </jmolButton> |
| </th> | | </jmol> |
| </tr> | | <jmol> |
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| <td> | | <script>anim off; frame 1.1</script> |
| <div style="font-size:120%; line-height:2.0em">Scientists and Students</div> | | <text>Wild Type</text> |
| </td> | | </jmolButton> |
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| <div style="font-size:120%; line-height:2.0em">Educators</div>
| | <jmol> |
| </td> | | <jmolButton> |
| <td> | | <script>anim off; frame 0</script> |
| <div style="font-size:120%; line-height:2.0em">Structural researchers</div> | | <text>Both</text> |
| </td> | | </jmolButton> |
| </tr> | | </jmol> |
| <tr> | | <jmol> |
| <td width="33%" valign="top"> | | <jmolButton> |
| * Understand and communicate protein 3D structure-function relationships
| | <script>if (~animation); if (_animating); anim pause; else; anim mode loop 0 0;anim fps 2; anim resume; endif; endif;</script> |
| ** Example: [[1wsu|Elongation factor SelB]], the protein responsible for adding the 21<sup>st</sup> amino acid selenocysteine to a growing protein chain in bacteria, as seen in the PDB's [[Teaching_Scenes%2C_Tutorials%2C_and_Educators%27_Pages#Molecule_of_the_Month_.28MotM.29_Series|Molecule of the Month]].
| | <text>Toggle Animation</text> |
| </td> | | </jmolButton> |
| <td width="34%" valign="top"> | | </jmol> |
| * Develop [[Teaching Scenes, Tutorials, and Educators' Pages|tutorials or molecular scenes]] to project during lectures
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| * [[Teaching Strategies Using Proteopedia|Assign students to construct pages]] in Proteopedia for [[Student Projects|class projects]] or reports
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| ''(You may [[Help:Protected Pages|protect your teaching pages from editing]] by others.)''
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| * Create [[3btp|supplementary material]] for your journal publications
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| * Create pages about your [[Research Groups|research team or institute]], highlighting structures you have researched.
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| ''(You may [[Help:Protected Pages|protect such pages from editing]] by others, or [[Proteopedia:Workbench|unwanted viewing]] pre-publication.)''
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| | Atoms are colored by element: |
| <table style="background: #D1FFE7; border:1px solid #94FFC8" cellspacing="5px" cellpadding="10px" width="100%">
| | {{Template:ColorKey_Element_C}}, |
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| | {{Template:ColorKey_Element_N}}, |
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| | {{Template:ColorKey_Element_O}} (in protein), |
| <div style="font-size:120%" align="left">Read the paper</div> | | <font color="magenta"><b>O</b></font> (in water). |
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| ''Proteopedia - a scientific 'wiki' bridging the rift between 3D structure and function of biomacromolecules'', '''Genome Biology''' 2008, 9:R121 [http://genomebiology.com/2008/9/8/R121 doi:10.1186/gb-2008-9-8-r121]
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