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Eric Martz's Favorites
From Proteopedia
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.
- 2004 - Lac repressor binding to DNA stabilizes a kink in 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.
- 2004 - The Bacterial Flagellar Hook, a molecular universal joint.
- 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.
See Also
- Atlas of Macromolecules -- an arbitrary list of beautiful, amazing, interesting and high-impact structures gathered by User:Eric Martz. It includes Magnificant Molecular Machines, Unusual Tertiary and Quaternary Structures, and over a dozen other categories containing over 150 PDB entries. Each structure is liked for further exploration in Proteopedia, FirstGlance in Jmol, and Protein Explorer.
- Highest impact structures which includes Structures saving the most lives.
