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4r0p

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'''Unreleased structure'''
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==Ifqins, an amyloid forming segment from human lysozyme spanning residues 56-61==
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<StructureSection load='4r0p' size='340' side='right' caption='[[4r0p]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4r0p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0P FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></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=4r0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r0p RCSB], [http://www.ebi.ac.uk/pdbsum/4r0p PDBsum]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Amyloid fibers, once exclusively associated with disease, are acquiring utility as a class of biological nanomaterials. Here we introduce a method that utilizes the atomic structures of amyloid peptides, to design materials with versatile applications. As a model application, we designed amyloid fibers capable of capturing carbon dioxide from flue gas, to address the global problem of excess anthropogenic carbon dioxide. By measuring dynamic separation of carbon dioxide from nitrogen, we show that fibers with designed amino acid sequences double the carbon dioxide binding capacity of the previously reported fiber formed by VQIVYK from Tau protein. In a second application, we designed fibers that facilitate retroviral gene transfer. By measuring lentiviral transduction, we show that designed fibers exceed the efficiency of polybrene, a commonly used enhancer of transduction. The same procedures can be adapted to the design of countless other amyloid materials with a variety of properties and uses.
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The entry 4r0p is ON HOLD
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Structure-based design of functional amyloid materials.,Li D, Jones EM, Sawaya MR, Furukawa H, Luo F, Ivanova M, Sievers SA, Wang W, Yaghi OM, Liu C, Eisenberg DS J Am Chem Soc. 2014 Dec 4. PMID:25474758<ref>PMID:25474758</ref>
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Authors: Sievers, S., Eisenberg, D.S., Sawaya, M.R.
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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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Description: Ifqins, an amyloid forming segment from human lysozyme spanning residues 56-61
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Lysozyme]]
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[[Category: Eisenberg, D S]]
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[[Category: Sawaya, M R]]
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[[Category: Sievers, S]]
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[[Category: Amyloid-like protofibril]]
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[[Category: Protein fibril]]

Revision as of 12:49, 17 December 2014

Ifqins, an amyloid forming segment from human lysozyme spanning residues 56-61

4r0p, resolution 1.52Å

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