3fr1

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==NFLVHS segment from Islet Amyloid Polypeptide (IAPP or Amylin)==
==NFLVHS segment from Islet Amyloid Polypeptide (IAPP or Amylin)==
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<StructureSection load='3fr1' size='340' side='right' caption='[[3fr1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='3fr1' size='340' side='right'caption='[[3fr1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3fr1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FR1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3fr1]] 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=3FR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FR1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 1.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fqp|3fqp]], [[3fth|3fth]], [[3ftk|3ftk]], [[3ftl|3ftl]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=3fr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fr1 OCA], [http://pdbe.org/3fr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fr1 RCSB], [http://www.ebi.ac.uk/pdbsum/3fr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fr1 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=3fr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fr1 OCA], [https://pdbe.org/3fr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fr1 RCSB], [https://www.ebi.ac.uk/pdbsum/3fr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fr1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 3fr1" 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: Amidation]]
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[[Category: Sawaya MR]]
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[[Category: Amyloid]]
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[[Category: Wiltzius JJW]]
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[[Category: Amyloid-like protofibril]]
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[[Category: Cleavage on pair of basic residue]]
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[[Category: Hormone]]
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[[Category: Polymorphism]]
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[[Category: Protein fibril]]
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[[Category: Secreted]]
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Current revision

NFLVHS segment from Islet Amyloid Polypeptide (IAPP or Amylin)

PDB ID 3fr1

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