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December 16, 2002
Volume 80, Number 50
CENEAR 80 50 pp. 41-42
ISSN 0009-2347



TWINS Chloride channel analyzed structurally by MacKinnon and coworkers contains two identical subunits (green and blue), each containing an anion pathway (red).
NMR ACCESSIBLE Wüthrich, Horwich, and coworkers used NMR to analyze the GroES component of this huge GroEL-GroES complex--about an order of magnitude larger than proteins previously accessible by solution NMR.
SIGLER & COWORKERS, NATURE, 388, 741 (1997)
William A. Goddard III of Caltech and coworkers developed and validated a set of computer programs capable of accurately predicting, from amino acid sequence data, the 3-D structure and binding characteristics of membrane proteins--which are normally difficult or impossible to analyze experimentally [Proc. Natl. Acad. Sci. USA, 99, 12622 (2002); C&EN, Oct. 14, page 14].

Roderick MacKinnon of Rockefeller University and coworkers determined the first atomic structure of a chloride-selective ion channel and proposed a mechanism of action [Nature, 415, 287 (2002); C&EN, Jan. 21, page 11]. Gatelike activity by a key glutamate may account for the channel's chloride selectivity.

The structure and mechanism of edema factor, which is the last of anthrax toxin's three protein components to be so analyzed, were determined by Wei-Jen Tang of the Ben May Institute for Cancer Research at the University of Chicago; Andrew Bohm of Boston Biomedical Research Institute, Watertown, Mass.; and coworkers [Nature, 415, 396 (2002); C&EN, Jan. 28, page 13].

The first crystal structures of G-quad-ruplexes formed from human telomeric DNA sequences were obtained by Stephen Neidle of the University of London and coworkers [Nature, 417, 876 (2002); C&EN, June 24, page 36]. Quadruplexes are potential anticancer targets.

By combining two NMR techniques, 2002 Nobel Prize in Chemistry winner Kurt Wüthrich of the Swiss Federal Institute of Technology, Arthur L. Horwich of Yale, and coworkers obtained supplementary information on the previously reported X-ray structure of the GroES component in the 900-kDa GroEL-GroES chaperonin complex [Nature, 418, 207 (2002); C&EN, July 15, page 9]. The complex is nearly an order of magnitude larger than proteins previously accessible by solution NMR.

A group led by Robert G. Griffin, Bruce Tidor, and Tomás Lozano-Pérez of MIT determined the atomic-resolution 3-D structure of a biomolecule by solid-state NMR for the first time [Proc. Natl. Acad. Sci. USA, 99, 10260 (2002); C&EN, Aug. 19, page 41].

In a high-resolution crystal structure of the MoFe protein of the nitrogen-fixing enzyme nitrogenase, Douglas C. Rees of California Institute of Technology (Caltech) and coworkers found a previously unrecognized atom--possibly nitrogen--coordinated to six iron atoms [Science, 297, 1696 (2002); C&EN, Sept. 9, page 9]. The discovery could aid efforts to design synthetic nitrogenase-like catalysts.

The microbial enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase, whose metal-ion components were believed to be only iron and nickel, turned out unexpectedly to contain copper as well. Catherine L. Drennan of MIT, Stephen W. Ragsdale of the University of Nebraska, Lincoln, and coworkers made the discovery [Science, 298, 567 (2002); C&EN, Oct. 21, page 13].

And in the area of rational design, John T. Koh of the University of Delaware and coworkers conceived and implemented an innovative therapeutic approach to vitamin D-resistant rickets [J. Am. Chem. Soc., 124, 13795 (2002); Org. Lett., 4, 3863 (2002); C&EN, Nov. 18, page 13]. They modified vitamin D to permit it to be recognized by a mutant vitamin D receptor that is found in some patients with the disease.


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