2bfi
From Proteopedia
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| - | [[Image:2bfi.png|left|200px]] | ||
| - | + | ==Molecular basis for amyloid fibril formation and stability== | |
| + | <StructureSection load='2bfi' size='340' side='right'caption='[[2bfi]], [[Resolution|resolution]] 1.10Å' 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]] 1.1Å</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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | <div class="pdbe-citations 2bfi" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Synthetic construct]] |
| - | [[Category: | + | [[Category: Atkins E]] |
| - | [[Category: | + | [[Category: Johansson J]] |
| - | + | [[Category: Makin OS]] | |
| + | [[Category: Serpell LC]] | ||
| + | [[Category: Sikorski P]] | ||
Current revision
Molecular basis for amyloid fibril formation and stability
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