2bfi: Difference between revisions

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[[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==
<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.
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]]
 
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