2li9

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[[Image:2li9.png|left|200px]]
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==Metal binding domain of rat beta-amyloid==
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<StructureSection load='2li9' size='340' side='right' caption='[[2li9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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[[2li9]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI9 OCA]. <br>
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<b>Related:</b> [[1ze7|1ze7]]<br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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In an attempt to reveal the mechanism of rats' resistance to Alzheimer's disease, we determined the structure of the metal-binding domain 1-16 of rat beta-amyloid (rat Abeta(1-16)) in solution in the absence and presence of zinc ions. A zinc-induced dimerization of the domain was detected. The zinc coordination site was found to involve residues His-6 and His-14 of both peptide chains. We used experimental restraints obtained from analyses of NMR and isothermal titration calorimetry data to perform structure calculations. The calculations employed an explicit water environment and a simulated annealing molecular-dynamics protocol followed by quantum-mechanical/molecular-mechanical optimization. We found that the C-tails of the two polypeptide chains of the rat Abeta(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Abeta dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat Abeta(1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer's disease.
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NMR solution structure of rat abeta(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease.,Istrate AN, Tsvetkov PO, Mantsyzov AB, Kulikova AA, Kozin SA, Makarov AA, Polshakov VI Biophys J. 2012 Jan 4;102(1):136-43. Epub 2012 Jan 3. PMID:22225807<ref>PMID:22225807</ref>
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The line below this paragraph, containing "STRUCTURE_2li9", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2li9| PDB=2li9 | SCENE= }}
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===Metal binding domain of rat beta-amyloid===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_22225807}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 22225807 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22225807}}
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==About this Structure==
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[[2li9]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI9 OCA].
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==Reference==
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<ref group="xtra">PMID:022225807</ref><ref group="xtra">PMID:021290829</ref><references group="xtra"/>
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[[Category: Istrate, A.]]
[[Category: Istrate, A.]]
[[Category: Kozin, S.]]
[[Category: Kozin, S.]]

Revision as of 08:37, 30 April 2014

Metal binding domain of rat beta-amyloid

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