Eric Martz's Favorites

(Difference between revisions)

Revision as of 21:37, 20 October 2008

1995-1997: Recoverin, a calcium-activated myristoyl switch. Calcium induces this protein to undergo a huge conformational change, literally turning one domain inside out. The N-terminal myristic acid goes from being buried within the hydrophobic core of a protein domain to being exposed, facilitating the attachment of this enzyme to disc membranes in rod cells in the eye. Morphs of this transition are shown.

2004 - Lac repressor binding to DNA bends the operator, due to sequence-specific hydrogen bonding opening the minor groove of the DNA. The solution of non-specific binding in 2004 (1osl) made possible a morph of the DNA bending during specific recognition by lac repressor.

2006 - Tamiflu bound to avian influenza neuraminidase N1, 2hu4 has tamiflu bound, while 2hty lacks this ligand. Tamiflu was designed for N2/N9, not N1. Its antiviral activity via N1 is fortunate but surprising. Comparison of these two structures shows that tamiflu pulls N1 loop 147-152 into close contact, a case of "induced fit". Another surprise was a cavity near tamiflu that could serve as a target for designing better anti-avian influenza drugs.
- For the full story, please see Avian Influenza Neuraminidase, Tamiflu and Relenza which includes a morph of the induced fit, and visualization of the cavity..
- Background slides for a lecture.
- Lesson plan on this topic.

To be added: MHC class I; domain-switched antibody; flagellar hook; dna-binding morph.

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 *1995-1997: [[Recoverin, a calcium-activated myristoyl switch]]. Calcium induces this protein to undergo a huge conformational change, literally turning one domain inside out. The N-terminal myristic acid goes from being buried within the hydrophobic core of a protein domain to being exposed, facilitating the attachment of this enzyme to disc membranes in rod cells in the eye. [[Morphs]] of this transition are [[Recoverin, a calcium-activated myristoyl switch|shown]].
+* 2004 - [[Lac repressor]] binding to DNA bends the operator, due to sequence-specific [[hydrogen bonds|hydrogen bonding]] opening the minor groove of the DNA. The solution of non-specific binding in 2004 ([[1osl]]) made possible a [[Lac repressor|morph of the DNA bending during specific recognition by lac repressor]].
 * 2006 - '''Tamiflu bound to avian influenza neuraminidase N1''', [[2hu4]] has tamiflu bound, while [[2hty]] lacks this ligand. Tamiflu was designed for N2/N9, not N1. Its antiviral activity via N1 is fortunate but surprising. Comparison of these two structures shows that tamiflu pulls N1 loop 147-152 into close contact, a case of "induced fit". Another surprise was a cavity near tamiflu that could serve as a target for designing better anti-avian influenza drugs.
 ** For the full story, please see [[Avian Influenza Neuraminidase, Tamiflu and Relenza]] which includes a morph of the induced fit, and visualization of the cavity..