by [list all teammate names here]
Student Projects for UMass Chemistry 423 Spring 2016
Overall Structure
The ligand binding domain of the aspartate receptor () ) is a dimer of two 4-helix bundles that is shown here with the bound.[2] 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.
Interactions that stabilize ligand binding[3] 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
- ↑ 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
- ↑ 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
- ↑ Milburn MV, Prive GG, Milligan DL, Scott WG, Yeh J, Jancarik J, Koshland DE Jr, Kim SH. Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science. 1991 Nov 29;254(5036):1342-7. PMID:1660187
