Home  

Random  

Nearby  



Log in  



Settings  



Donate  



About Wikipedia  

Disclaimers  



Wikipedia





User:Daamoy/sandbox: Difference between revisions





User page  

Talk  



Language  

Watch  

View history  

Edit  






Browse history interactively
 Previous editNext edit 
Content deleted Content added
VisualWikitext
Daamoy (talk | contribs)
183 edits
Daamoy (talk | contribs)
183 edits
Line 16:
* Eight transmembrane segments that form a channel and allow for copper to pass through the membrane;
* An ATP-binding domain;
* A large N-terminal cytosolic domain that contains six tandemly repeated copper-binding sites of about 30 amino acids, each containing a GMTCXXC motif.<ref name="5.Cellular multitasking: The dual role">{{cite journal|last1=Lutsenko|first1=Svetlana|last2=Gupta|first2=Arnab|last3=Burkhead|first3=Jason L.|last4=Zuzel|first4=Vesna|title=Cellular multitasking: The dual role of human Cu-ATPases in cofactor delivery and intracellular copper balance|journal=Archives of Biochemistry and Biophysics|date=August 2008|volume=476|issue=1|pages=22–32|doi=10.1016/j.abb.2008.05.005}}</ref><ref name="1.Copper-related diseases: From chemistry">{{cite journal|last1=Crisponi|first1=Guido|last2=Nurchi|first2=Valeria Marina|last3=Fanni|first3=Daniela|last4=Gerosa|first4=Clara|last5=Nemolato|first5=Sonia|last6=Faa|first6=Gavino|title=Copper-related diseases: From chemistry to molecular pathology|journal=Coordination Chemistry Reviews|date=April 2010|volume=254|issue=7-8|pages=876–889|doi=10.1016/j.ccr.2009.12.018}}</ref><ref name="Textbook NEW">{{cite book|last1=Bertini|first1=Ivano|last2=Gray|first2=Harry|last3=Stiefel|first3=Edward|last4=Valentine|first4=Joan|title=Biological inorganic chemistry : structure and reactivity.|date=2006|publisher=University Science Books|location=Sausalito, CA|isbn=978-1-891389-43-6}}</ref><ref name=3.>{{cite journal|last1=Inesi|first1=Giuseppe|last2=Pilankatta|first2=Rajendra|last3=Tadini‑Buoninsegni|first3=Francesco|title=Biochemical characterization of P-type copper ATPases|journal=Biochemical Journal|date=15 October 2014|volume=463|issue=2|pages=167–176|doi=10.1042/BJ20140741}}</ref>
 
Many motifs in the ATP7A structure are conserved, such as the TGEA, CPC, DKTG, SEHPL, and GDGXND motifs. The TGEA motif lies in the loop on the cytosolic side between transmembrane segments 4 and 5 and is involved in energy transduction. The CPC motif located in transmembrane segment 6 is common for all heavy metal transporting ATPases. Between transmembrane segments 6 and 7 is a large cytoplasmic loop, where three motifs are located: DKTG, SEHPL, and GDGXND. The DKTG motif is essential for the proper function of the ATPase. The [[aspartic acid]] (D) residue is phosphorylated during the transport cycles. The SEHPL motif only exists in heavy metal transporting P-type ATPases. Without the [[histidine]] (H) residue ATP7A may not function properly. The GDGXND motif near transmembrane segment 7 is thought to contain mainly α-helices and serves as a structural support.<ref name="Textbook NEW" />

Retrieved from "https://en.wikipedia.org/wiki/User:Daamoy/sandbox"
 




Languages

 



This page is not available in other languages.
 

Wikipedia




Privacy policy

About Wikipedia

Disclaimers

Contact Wikipedia

Code of Conduct

Developers

Statistics

Cookie statement

Terms of Use

Desktop