Nucleoplasmin: Difference between revisions

No edit summary
No edit summary
Line 15: Line 15:
the NP in Humans is made out of <scene name='46/467273/Dimer/1'>dimer</scene> while each <scene name='46/467273/Monomer/2'>monomer</scene> consisted of five chains. The structure remain similiar to the one in Xenopus but with a change in amino acids in its <scene name='46/467273/Core_domain/2'>core domain</scene>, Val insted of Ile.  
the NP in Humans is made out of <scene name='46/467273/Dimer/1'>dimer</scene> while each <scene name='46/467273/Monomer/2'>monomer</scene> consisted of five chains. The structure remain similiar to the one in Xenopus but with a change in amino acids in its <scene name='46/467273/Core_domain/2'>core domain</scene>, Val insted of Ile.  
The Decamer bind H2A-H2B dimers and H3-H4 tetramers simultaneously, In the absence of histone tetramers the pentamer binds H2A-H2B and formes central hub. When H3-H4 tetramers are recruited this results in a functional dimerization of the complex, and the decamer being formed.
The Decamer bind H2A-H2B dimers and H3-H4 tetramers simultaneously, In the absence of histone tetramers the pentamer binds H2A-H2B and formes central hub. When H3-H4 tetramers are recruited this results in a functional dimerization of the complex, and the decamer being formed.
== conservastion ==
The loop in the core domain of Xenopus NP is not highly conserved, [[Image:1k5j.png | thumb | Xenopus]]
while the core domain in human is more conserved compared to Xenopus. [[Image:3T30.png | thumb | Human]]
[[Image:1-s2.0-S0022519316001053-gr5.jpg]]
The general structure remain similiar, even with changes in amino acids in the core domains between the two species. That can point to the fact they have similar roles as a molecular chaperone in Human and Xenopus.


==3D structures of nucleoplasmin==
==3D structures of nucleoplasmin==
Line 35: Line 59:
4. SHU Te-Jun, ZHANG Yao-Zhou. Nucleoplasmin, an Important Nuclear Chaperone. Chinese Journal of Biochemistry and Molecular Biol. 15 March 2007  http://cjbmb.bjmu.edu.cn/EN/Y2007/V23/I09/718  
4. SHU Te-Jun, ZHANG Yao-Zhou. Nucleoplasmin, an Important Nuclear Chaperone. Chinese Journal of Biochemistry and Molecular Biol. 15 March 2007  http://cjbmb.bjmu.edu.cn/EN/Y2007/V23/I09/718  
[[Category:Topic Page]]
[[Category:Topic Page]]
5. Platonova, O., Akey, I.V., Head, J.F., Akey, C.W.Crystal structure and function of human nucleoplasmin (npm2): a histone chaperone in oocytes and embryos.Biochemistry.2011 Sep 20;50(37):8078-89.
PMCID:PMC3172369 DOI:10.1021/bi2006652

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Jaime Prilusky, Tomer Gelman