2bp4
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2bp4.gif|left|200px]] | [[Image:2bp4.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2bp4", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2bp4| PDB=2bp4 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''ZINC-BINDING DOMAIN OF ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE IN TFE-WATER (80-20) SOLUTION''' | '''ZINC-BINDING DOMAIN OF ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE IN TFE-WATER (80-20) SOLUTION''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BP4 is a [[Single protein]] structure | + | 2BP4 is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1o6n 1o6n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BP4 OCA]. |
==Reference== | ==Reference== | ||
| Line 33: | Line 30: | ||
[[Category: Zirah, S.]] | [[Category: Zirah, S.]] | ||
[[Category: 3d-structure,helix]] | [[Category: 3d-structure,helix]] | ||
| - | [[Category: | + | [[Category: Alzheimer's disease]] |
| - | [[Category: | + | [[Category: Amyloid]] |
| - | [[Category: | + | [[Category: Amyloid peptide]] |
| - | [[Category: | + | [[Category: Beta-amyloid protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:36:02 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:36, 3 May 2008
ZINC-BINDING DOMAIN OF ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE IN TFE-WATER (80-20) SOLUTION
Overview
Amyloid deposits within the cerebral tissue constitute a characteristic lesion associated with Alzheimer disease. They mainly consist of the amyloid peptide Abeta and display an abnormal content in Zn(2+) ions, together with many truncated, isomerized, and racemized forms of Abeta. The region 1-16 of Abeta can be considered the minimal zinc-binding domain and contains two aspartates subject to protein aging. The influence of zinc binding and protein aging related modifications on the conformation of this region of Abeta is of importance given the potentiality of this domain to constitute a therapeutic target, especially for immunization approaches. In this study, we determined from NMR data the solution structure of the Abeta-(1-16)-Zn(2+) complex in aqueous solution at pH 6.5. The residues His(6), His(13), and His(14) and the Glu(11) carboxylate were identified as ligands that tetrahedrally coordinate the Zn(II) cation. In vitro aging experiments on Abeta-(1-16) led to the formation of truncated and isomerized species. The major isomer generated, Abeta-(1-16)-l-iso-Asp(7), displayed a local conformational change in the His(6)-Ser(8) region but kept a zinc binding propensity via a coordination mode involving l-iso-Asp(7). These results are discussed here with regard to Abeta fibrillogenesis and the potentiality of the region 1-16 of Abeta to be used as a therapeutic target.
About this Structure
2BP4 is a Single protein structure. This structure supersedes the now removed PDB entry 1o6n. Full crystallographic information is available from OCA.
Reference
Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging., Zirah S, Kozin SA, Mazur AK, Blond A, Cheminant M, Segalas-Milazzo I, Debey P, Rebuffat S, J Biol Chem. 2006 Jan 27;281(4):2151-61. Epub 2005 Nov 21. PMID:16301322 Page seeded by OCA on Sat May 3 20:36:02 2008
