Eric Martz's Favorites
From Proteopedia
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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]]. | *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]]. | ||
* 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. | * 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. | ||
| - | ** [http://www.umass.edu/molvis/martz/lectures/ | + | ** 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.. |
| - | ** [http://www.umass.edu/molvis/martz/lectures/ | + | ** [http://www.umass.edu/molvis/martz/lectures/labmolgen/n1tami.htm Background] slides for a lecture. |
| - | + | ** [http://www.umass.edu/molvis/martz/lectures/labmolgen/index.htm Lesson plan on this topic]. | |
| - | + | ||
To be added: MHC class I; domain-switched antibody; flagellar hook; dna-binding morph. | To be added: MHC class I; domain-switched antibody; flagellar hook; dna-binding morph. | ||
Revision as of 21:32, 20 October 2008
Eric Martz's Favorites
- 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.
- 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.
