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Cu(I) Binding to Designed Proteins Reveals a Putative Copper Binding Site of the Human Line1 Retrotransposon Protein ORF1p

Journal Article · · Inorganic Chemistry
 [1];  [1];  [2];  [2];  [1]
  1. Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, United States
  2. Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, United States; Program in Biophysics, University of Michigan, Ann Arbor, Michigan 48109, United States
+ Show Author Affiliations
Not provided.
Research Organization:
SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC02-76SF00515
OSTI ID:
1981857
Journal Information:
Inorganic Chemistry, Journal Name: Inorganic Chemistry Journal Issue: 12 Vol. 61; ISSN 0020-1669
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English

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C-Terminal Domain of the Membrane Copper Transporter Ctr1 from Saccharomyces cerevisiae Binds Four Cu(I) Ions as a Cuprous-Thiolate Polynuclear Cluster:  Sub-femtomolar Cu(I) Affinity of Three Proteins Involved in Copper Trafficking journal March 2004
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