2kn6

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[[Image:2kn6.png|left|200px]]
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==Structure of full-length human ASC (Apoptosis-associated speck-like protein containing a CARD)==
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<StructureSection load='2kn6' size='340' side='right' caption='[[2kn6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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[[2kn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KN6 OCA]. <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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|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/kn/2kn6_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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
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The human protein ASC is a key mediator in apoptosis and inflammation. Through its two death domains (pyrin and CARD) ASC interacts with cell death executioners, acts as an essential adapter for inflammasome integrity, and oligomerizes into functional supramolecular assemblies. However, these functions are not understood at the structural-dynamic level. This study reports the solution structure and interdomain dynamics of full-length ASC. The pyrin and CARD domains are structurally independent six-helix bundle motifs connected by a 23-residue linker. The CARD structure reveals two distinctive characteristics; helix 1 is not fragmented as in all other known CARDs, and its electrostatic surface shows a uniform distribution of positive and negative charges, whereas these are commonly separated into two areas in other death domains. The linker adopts residual structure resulting in a back-to-back orientation of the domains, which avoids steric interference of each domain with the binding site of the other. NMR relaxation experiments show that the linker is flexible despite the residual structure. This flexibility could help expand the relative volume occupied by each domain, thus increasing the capture radius for effectors. Based on the ASC structure, a tentative model is proposed to illustrate how ASC oligomerizes via CARD and pyrin homophilic interactions. Moreover, ASC oligomers have been analyzed by atomic force microscopy, showing a predominant species of disk-like particles of approximately 12-nm diameter and approximately 1-nm height. Taken together, these results provide structural insight into the behavior of ASC as an adapter molecule.
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Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC).,de Alba E J Biol Chem. 2009 Nov 20;284(47):32932-41. Epub 2009 Sep 15. PMID:19759015<ref>PMID:19759015</ref>
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The line below this paragraph, containing "STRUCTURE_2kn6", 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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-->
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{{STRUCTURE_2kn6| PDB=2kn6 | SCENE= }}
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===Structure of full-length human ASC (Apoptosis-associated speck-like protein containing a CARD)===
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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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__TOC__
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The line below this paragraph, {{ABSTRACT_PUBMED_19759015}}, 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 19759015 is the PubMed ID number.
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-->
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{{ABSTRACT_PUBMED_19759015}}
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==About this Structure==
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[[2kn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KN6 OCA].
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==Reference==
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<ref group="xtra">PMID:019759015</ref><ref group="xtra">PMID:019636848</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Alba, E De.]]
[[Category: Alba, E De.]]

Revision as of 08:20, 30 April 2014

Structure of full-length human ASC (Apoptosis-associated speck-like protein containing a CARD)

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