Sandbox Reserved 439

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=='''Asp Receptor Ligand-binding domain (1wat)<ref>PMID: 8486661</ref>'''==
=='''Asp Receptor Ligand-binding domain (1wat)<ref>PMID: 8486661</ref>'''==
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This is an example page. Edit appropriately for your project.
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<font color='green'>This is an example page. Edit appropriately for your project. Upon completion, delete instructions in green.
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1. Add a citation to the primary reference at the end of the title above: you should all read this paper!
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Edit the title section to add the command <ref>PMID: xxx</ref> following the pdb code.
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Go to [http://www.rcsb.org/pdb/home/home.do] and search for your pdb code.
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Go down to the abstract and click "Search on Pubmed".
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In pubmed, copy the PMID code you see right below the abstract, and paste it to replace the code in the <ref> command.
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</font>
<StructureSection load='1wat' size='350' side='right' caption='Bacteria use this protein to "smell" their environment (PDB entry [[1wat]])' scene=''>
<StructureSection load='1wat' size='350' side='right' caption='Bacteria use this protein to "smell" their environment (PDB entry [[1wat]])' scene=''>

Revision as of 18:18, 2 March 2016


This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439.



Contents

Asp Receptor Ligand-binding domain (1wat)[1]

This is an example page. Edit appropriately for your project. Upon completion, delete instructions in green.

1. Add a citation to the primary reference at the end of the title above: you should all read this paper! Edit the title section to add the command [2] following the pdb code. Go to [1] and search for your pdb code. Go down to the abstract and click "Search on Pubmed". In pubmed, copy the PMID code you see right below the abstract, and paste it to replace the code in the [3] In this the N and C termini are at the bottom of the structure; this is where the connections to the transmembrane helices have been truncated.

Binding Interactions

When the protein is colored according to , residues at the ligand site are the most conserved. Image:ColorKey ConSurf NoYellow.gif

Interactions that stabilize ligand binding[4] include hydrogen bonding from Tyr149 and Gln152 backbone carbonyls and Thr154 sidechain OH to the and hydrogen bonding from the sidechain nitrogens of Arg64, Arg69, and Arg73 to the two .

Additional Features

Quiz Question 1

See Also

Credits

Introduction - name of team member

Overall Structure - name of team member

Binding Interactions - name of team member

Additional Features - name of team member

Quiz Question 1 - name of team member

References

  1. ↑ Yeh JI, Biemann HP, Pandit J, Koshland DE, Kim SH. The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J Biol Chem. 1993 May 5;268(13):9787-92. PMID:8486661
  2. ↑ PMID: xxx
  3. ↑ command. </font>

    Bacteria use this protein to "smell" their environment (PDB entry 1wat)

    Drag the structure with the mouse to rotate

</StructureSection>

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