2bfi: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
New page: left|200px<br /><applet load="2bfi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bfi, resolution 1.1Å" /> '''MOLECULAR BASIS FOR A...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2bfi.gif|left|200px]]<br /><applet load="2bfi" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bfi, resolution 1.1&Aring;" />
'''MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY'''<br />


==Overview==
==Molecular basis for amyloid fibril formation and stability==
The molecular structure of the amyloid fibril has remained elusive because, of the difficulty of growing well diffracting crystals. By using a, sequence-designed polypeptide, we have produced crystals of an amyloid, fiber. These crystals diffract to high resolution (1 A) by electron and, x-ray diffraction, enabling us to determine a detailed structure for, amyloid. The structure reveals that the polypeptides form fibrous crystals, composed of antiparallel beta-sheets in a cross-beta arrangement, characteristic of all amyloid fibers, and allows us to determine the, side-chain packing within an amyloid fiber. The antiparallel beta-sheets, are zipped together by means of pi-bonding between adjacent phenylalanine, rings and salt-bridges between charge pairs (glutamic acid-lysine), thus, controlling and stabilizing the structure. These interactions are likely, to be important in the formation and stability of other amyloid fibrils.
<StructureSection load='2bfi' size='340' side='right'caption='[[2bfi]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bfi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfi OCA], [https://pdbe.org/2bfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfi RCSB], [https://www.ebi.ac.uk/pdbsum/2bfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfi ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high resolution (1 A) by electron and x-ray diffraction, enabling us to determine a detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel beta-sheets in a cross-beta arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. The antiparallel beta-sheets are zipped together by means of pi-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid-lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.


==About this Structure==
Molecular basis for amyloid fibril formation and stability.,Makin OS, Atkins E, Sikorski P, Johansson J, Serpell LC Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):315-20. Epub 2005 Jan 3. PMID:15630094<ref>PMID:15630094</ref>
2BFI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFI OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Molecular basis for amyloid fibril formation and stability., Makin OS, Atkins E, Sikorski P, Johansson J, Serpell LC, Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):315-20. Epub 2005 Jan 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15630094 15630094]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 2bfi" style="background-color:#fffaf0;"></div>
[[Category: Atkins, E.]]
== References ==
[[Category: Johansson, J.]]
<references/>
[[Category: Makin, O.Sumner.]]
__TOC__
[[Category: Serpell, L.C.]]
</StructureSection>
[[Category: Sikorski, P.]]
[[Category: Large Structures]]
[[Category: amyloid]]
[[Category: Synthetic construct]]
[[Category: beta-sheet interactions]]
[[Category: Atkins E]]
[[Category: electron diffraction]]
[[Category: Johansson J]]
[[Category: fiber diffraction]]
[[Category: Makin OS]]
[[Category: pi-pi bonding]]
[[Category: Serpell LC]]
[[Category: x-ray diffraction]]
[[Category: Sikorski P]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:23:16 2008''
Retrieved from "https://proteopedia.org/2bfi"