3ftk

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==NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), hydrated crystal form==
==NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), hydrated crystal form==
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<StructureSection load='3ftk' size='340' side='right' caption='[[3ftk]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='3ftk' size='340' side='right'caption='[[3ftk]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ftk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FTK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ftk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FTK FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fod|3fod]], [[3fpo|3fpo]], [[3fqp|3fqp]], [[3fr1|3fr1]], [[3fth|3fth]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ftk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftk OCA], [http://pdbe.org/3ftk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ftk RCSB], [http://www.ebi.ac.uk/pdbsum/3ftk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ftk ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ftk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftk OCA], [https://pdbe.org/3ftk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ftk RCSB], [https://www.ebi.ac.uk/pdbsum/3ftk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ftk ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/IAPP_HUMAN IAPP_HUMAN] Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
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In prion inheritance and transmission, strains are phenotypic variants encoded by protein 'conformations'. However, it is unclear how a protein conformation can be stable enough to endure transmission between cells or organisms. Here we describe new polymorphic crystal structures of segments of prion and other amyloid proteins, which offer two structural mechanisms for the encoding of prion strains. In packing polymorphism, prion strains are encoded by alternative packing arrangements (polymorphs) of beta-sheets formed by the same segment of a protein; in segmental polymorphism, prion strains are encoded by distinct beta-sheets built from different segments of a protein. Both forms of polymorphism can produce enduring conformations capable of encoding strains. These molecular mechanisms for transfer of protein-encoded information into prion strains share features with the familiar mechanism for transfer of nucleic acid-encoded information into microbial strains, including sequence specificity and recognition by noncovalent bonds.
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Molecular mechanisms for protein-encoded inheritance.,Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D Nat Struct Mol Biol. 2009 Sep;16(9):973-8. Epub 2009 Aug 16. PMID:19684598<ref>PMID:19684598</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ftk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eisenberg, D]]
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[[Category: Homo sapiens]]
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[[Category: Sawaya, M R]]
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[[Category: Large Structures]]
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[[Category: Wiltzius, J J.W]]
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[[Category: Eisenberg D]]
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[[Category: Amyloid-like protofibril]]
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[[Category: Sawaya MR]]
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[[Category: Protein fibril]]
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[[Category: Wiltzius JJW]]

Current revision

NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), hydrated crystal form

PDB ID 3ftk

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