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Journal home Advance online publication Current issue Archive Press releases Supplements Focus Guide to authors Online submission Permissions For referees Free online issue Contact the journal Subscribe Advertising work@npg naturereprints About this site For librarians   NPG Resources Nature Nature Cell Biology Nature Reviews Molecular Cell Biology The EMBO Journal Nature Reports Avian Flu NPG Subject areas Biotechnology Cancer Chemistry Clinical Medicine Dentistry Development Drug Discovery Earth Sciences Evolution & Ecology Genetics Immunology Materials Science Medical Research Microbiology Molecular Cell Biology Neuroscience Pharmacology Physics Browse all publications Article Nature Structural Biology  5, 47 - 54 (1998) doi:10.1038/nsb0198-47 Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase Jane Gitschier1, Barbara Moffat2, Dorothea Reilly3, William I. Wood4 & Wayne J. Fairbrother5   1Howard Hughes Medical Institute and Departments of Medicine and Pediatrics, University of California, San Francisco, California 94143, USA.   2Department of Protein Chemistry, Genentech, Inc., South San Francisco, California 90480, USA.   3Department of Cell Culture, Genentech, Inc., South San Francisco, California 90480, USA.   4Department of Molecular Biology, Genentech, Inc., South San Francisco, California 90480, USA.   5Department of Protein Engineering, Genentech, Inc., South San Francisco, California 90480, USA. e-mail: fairbro@gene.com Menkes disease is an X-linked disorder in copper transport that results in death during early childhood. The solution structures of both apo and Ag(l)-bound forms of the fourth metal-binding domain (mbd4) from the Menkes copper-transporting ATPase have been solved. The 72-residue mbd4 has a ferredoxin-like fold. Structural differences between the two forms are limited to the metal-binding loop, which is disordered in the apo structure but well ordered in the Ag(l)-bound structure. Ag(l) binds in a linear bicoordinate manner to the two Cys residues of the conserved GMTCxxC motif; Cu(l) likely coordinates in a similar manner. Menkes mbd4 is thus the first bicoordinate copper-binding protein to be characterized structurally. Sequence comparisons with other heavy-metal-binding domains reveal a conserved hydrophobic core and metal-binding motif.  Top Abstract Previous | Next Table of contents Full text Download PDF Send to a friend Save this link Open Innovation Challenges Methods of Modeling Adaptation in Populations Deadline: Dec 30 2009 Reward: $15,000 USD The analysis of adaptation with a population is a frequently encountered computational modeling scen... Novel Approaches to Protecting Maize from Insect Damage Deadline: Jan 31 2010 Reward: $20,000 USD The Seeker is looking for novel approaches to protecting maize from insect damage. This Challenge re... More Challenges Powered by: nature jobs Professor of Experimental Virology (W3) University Hospital Jena, Institute of Virology and Antivirale Therapy Jena, Germany Post Doctoral Positions Italian Institute of Technology (IIT) Lecce Italy More science jobs Post a job for free Export citation Search buyers guide:   ADVERTISEMENT

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