1nmj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nmj.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1nmj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nmj| PDB=1nmj | SCENE= }}
{{STRUCTURE_1nmj| PDB=1nmj | SCENE= }}
-
'''The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain'''
+
===The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain===
-
==Overview==
+
<!--
-
The amyloid beta-peptide (Abeta) is a major component of insoluble amyloid deposits in Alzheimer's disease, and the ability of the beta-peptide to exist in different conformations is dependent on residues 1-28 [beta-(1-28)]. However, different from humans, no Abeta amyloid deposition has been found in aged rats' brains. Studying the three-dimensional solution structure of rat Abeta-(1-28) and the binding circumstance of Zn(2+) is beneficial to a clear understanding of the potential role of Zn(2+) in Alzheimer-associated neuropathogenesis and to suggest why there is no amyloid deposition in aged rats' brains. Here we used nuclear magnetic resonance (NMR) spectroscopy to determine the solution structure of rat Abeta-(1-28) and the binding constant of Zn(2+) to rat Abeta-(1-28). Our results suggest that (1) the three-dimensional solution structure of rat Abeta-(1-28) is more stable than that of human Abeta-(1-28) in DMSO- d(6) and that a helical region from Glu16 to Val24 exists in the rat Abeta-(1-28); (2) the affinity of Zn(2+) for rat Abeta-(1-28) is lower than that for human Abeta-(1-28) and the NMR data suggest that Arg13, His6, and His14 residues provide the primary binding sites for Zn(2+); and (3) the proper binding of Zn(2+) to rat Abeta-(1-28) can induce the peptide to change to a more stable conformation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15160315}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15160315 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15160315}}
==About this Structure==
==About this Structure==
-
1NMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA].
+
1NMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Amyloid]]
[[Category: Amyloid]]
[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:42:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:49:49 2008''

Revision as of 06:49, 28 July 2008

Image:1nmj.png

Template:STRUCTURE 1nmj

The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain

Template:ABSTRACT PUBMED 15160315

About this Structure

1NMJ is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

Reference

The solution structure of rat Abeta-(1-28) and its interaction with zinc ion: insights into the scarcity of amyloid deposition in aged rat brain., Huang J, Yao Y, Lin J, Ye YH, Sun WY, Tang Dagger WX, J Biol Inorg Chem. 2004 Jul;9(5):627-35. Epub 2004 May 25. PMID:15160315

Page seeded by OCA on Mon Jul 28 09:49:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nmj"
Personal tools