From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1x1p.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1x1p.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1x1p| PDB=1x1p | SCENE= }} | | {{STRUCTURE_1x1p| PDB=1x1p | SCENE= }} |
| | | | |
| - | '''Crystal structure of Tk-RNase HII(1-197)-A(28-42)'''
| + | ===Crystal structure of Tk-RNase HII(1-197)-A(28-42)=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Conformational studies on amyloid beta peptide (Abeta) in aqueous solution are complicated by its tendency to aggregate. In this study, we determined the atomic-level structure of Abeta(28-42) in an aqueous environment. We fused fragments of Abeta, residues 10-24 (Abeta(10-24)) or 28-42 (Abeta(28-42)), to three positions in the C-terminal region of ribonuclease HII from a hyperthermophile, Thermococcus kodakaraensis (Tk-RNase HII). We then examined the structural properties in an aqueous environment. The host protein, Tk-RNase HII, is highly stable and the C-terminal region has relatively little interaction with other parts. CD spectroscopy and thermal denaturation experiments demonstrated that the guest amyloidogenic sequences did not affect the overall structure of the Tk-RNase HII. Crystal structure analysis of Tk-RNase HII(1-197)-Abeta(28-42) revealed that Abeta(28-42) forms a beta conformation, whereas the original structure in Tk-RNase HII(1-213) was alpha helix, suggesting beta-structure formation of Abeta(28-42) within full-length Abeta in aqueous solution. Abeta(28-42) enhanced aggregation of the host protein more strongly than Abeta(10-24). These results and other reports suggest that after proteolytic cleavage, the C-terminal region of Abeta adopts a beta conformation in an aqueous environment and induces aggregation, and that the central region of Abeta plays a critical role in fibril formation. This study also indicates that this fusion technique is useful for obtaining structural information with atomic resolution for amyloidogenic peptides in aqueous environments.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16367755}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16367755 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16367755}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Ribonuclease hii]] | | [[Category: Ribonuclease hii]] |
| | [[Category: Thermococcus kodakaraensis]] | | [[Category: Thermococcus kodakaraensis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:25:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:01:59 2008'' |
Revision as of 09:02, 29 July 2008
Template:STRUCTURE 1x1p
Crystal structure of Tk-RNase HII(1-197)-A(28-42)
Template:ABSTRACT PUBMED 16367755
About this Structure
1X1P is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.
Reference
Structure of amyloid beta fragments in aqueous environments., Takano K, Endo S, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S, FEBS J. 2006 Jan;273(1):150-8. PMID:16367755
Page seeded by OCA on Tue Jul 29 12:01:59 2008
