3g7v

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[[Image:3g7v.png|left|200px]]
 
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{{STRUCTURE_3g7v| PDB=3g7v | SCENE= }}
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==Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein==
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<StructureSection load='3g7v' size='340' side='right'caption='[[3g7v]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3g7v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G7V FirstGlance]. <br>
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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]] 1.86&#8491;</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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3g7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g7v OCA], [https://pdbe.org/3g7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g7v RCSB], [https://www.ebi.ac.uk/pdbsum/3g7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g7v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g7/3g7v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3g7v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Islet Amyloid Polypeptide (IAPP or amylin) is a peptide hormone produced and stored in the beta-islet cells of the pancreas along with insulin. IAPP readily forms amyloid fibrils in vitro, and the deposition of fibrillar IAPP has been correlated with the pathology of type II diabetes. The mechanism of the conversion that IAPP undergoes from soluble to fibrillar forms has been unclear. By chaperoning IAPP through fusion to maltose binding protein, we find that IAPP can adopt a alpha-helical structure at residues 8-18 and 22-27 and that molecules of IAPP dimerize. Mutational analysis suggests that this dimerization is on the pathway to fibrillation. The structure suggests how IAPP may heterodimerize with insulin, which we confirmed by protein crosslinking. Taken together, these experiments suggest the helical dimerization of IAPP accelerates fibril formation and that insulin impedes fibrillation by blocking the IAPP dimerization interface.
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===Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein===
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Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process.,Wiltzius JJ, Sievers SA, Sawaya MR, Eisenberg D Protein Sci. 2009 Apr 29. PMID:19475663<ref>PMID:19475663</ref>
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{{ABSTRACT_PUBMED_19475663}}
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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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==About this Structure==
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<div class="pdbe-citations 3g7v" style="background-color:#fffaf0;"></div>
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[[3g7v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7V OCA].
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== References ==
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<references/>
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==See Also==
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__TOC__
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*[[Maltose-binding protein|Maltose-binding protein]]
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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==Reference==
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<ref group="xtra">PMID:019475663</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Eisenberg, D.]]
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[[Category: Large Structures]]
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[[Category: Sawaya, M R.]]
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[[Category: Eisenberg D]]
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[[Category: Wiltzius, J J.W.]]
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[[Category: Sawaya MR]]
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[[Category: Amidation]]
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[[Category: Wiltzius JJW]]
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[[Category: Amyloid]]
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[[Category: Cleavage on pair of basic residue]]
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[[Category: Hormone]]
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[[Category: Native fold for amyloidogenic protein]]
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[[Category: Secreted]]
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[[Category: Sugar binding protein]]
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[[Category: Sugar transport]]
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[[Category: Transport]]
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Current revision

Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein

PDB ID 3g7v

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