3g7w

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'''Unreleased structure'''
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{{Seed}}
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[[Image:3g7w.jpg|left|200px]]
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The entry 3g7w is ON HOLD until Paper Publication
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{{STRUCTURE_3g7w| PDB=3g7w | SCENE= }}
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Authors: Wiltzius, J.J.W., Sawaya, M.R., Eisenberg, D.
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===Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein===
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Description: Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 4 14:44:52 2009''
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The line below this paragraph, {{ABSTRACT_PUBMED_19475663}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 19475663 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19475663}}
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==About this Structure==
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3G7W is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_homo_sapiens Escherichia coli, homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7W OCA].
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==Reference==
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<ref group="xtra">PMID:19475663</ref><references group="xtra"/>
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[[Category: Escherichia coli, homo sapiens]]
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[[Category: Eisenberg, D.]]
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[[Category: Sawaya, M R.]]
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[[Category: Wiltzius, J J.W.]]
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[[Category: Amidation]]
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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: Periplasm]]
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[[Category: Polymorphism]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 25 09:08:35 2009''

Revision as of 06:08, 25 June 2009

Template:STRUCTURE 3g7w

Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein

Template:ABSTRACT PUBMED 19475663

About this Structure

3G7W is a 1 chain structure of sequence from Escherichia coli, homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Wiltzius JJ, Sievers SA, Sawaya MR, Eisenberg D. Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process. Protein Sci. 2009 Apr 29. PMID:19475663 doi:10.1002/pro.145

Page seeded by OCA on Thu Jun 25 09:08:35 2009

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