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1qzp

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(New page: 200px<br /> <applet load="1qzp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qzp" /> '''NMR structure of the human dematin headpiec...)
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[[Image:1qzp.gif|left|200px]]<br />
 
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<applet load="1qzp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qzp" />
 
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'''NMR structure of the human dematin headpiece domain'''<br />
 
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==Overview==
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==NMR structure of the human dematin headpiece domain==
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Dematin (band 4.9) is found in the junctional complex of the spectrin, cytoskeleton that supports the erythrocyte cell membrane. Dematin is a, member of the larger class of cytoskeleton-associated proteins that, contain a modular "headpiece" domain at their extreme C termini. The, dematin headpiece domain provides the second F-actin-binding site required, for in vitro F-actin bundling. The dematin headpiece is found in two forms, in the cell, one of 68 residues (DHP) and one containing a 22-amino acid, insert near its N terminus (DHP+22). In addition, dematin contains the, only headpiece domain that is phosphorylated, in vivo. The 22-amino acid, insert in DHP+22 appeared unstructured in NMR spectra; therefore, we have, determined the three-dimensional structure of DHP by multidimensional NMR, methods. Although the overall three-dimensional structure of DHP is, similar to that of the villin headpiece, there are two novel, characteristics revealed by this structure. First, unlike villin headpiece, that contains a single buried salt bridge, DHP contains a buried charged, cluster comprising residues Glu(39), Arg(66), Lys(70), and the C-terminal, carboxylate of Phe(76). Second, (15)N relaxation experiments indicate that, the longer "variable loop" region near the N terminus of DHP (residues, 20-29) is dynamic, undergoing significantly greater motions that the rest, of the structure. Furthermore, NMR chemical shift changes indicate that, the conformation of the dynamic variable loop is altered by, phosphorylation of serine 74, which is far in the sequence from the, variable loop region. Our results suggest that phosphorylation of the, dematin headpiece acts as a conformational switch within this headpiece, domain.
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<StructureSection load='1qzp' size='340' side='right'caption='[[1qzp]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qzp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZP 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">Solution NMR</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=1qzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzp OCA], [https://pdbe.org/1qzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qzp RCSB], [https://www.ebi.ac.uk/pdbsum/1qzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEMA_HUMAN DEMA_HUMAN] Actin-bundling protein. May function in mitogen-activated protein kinase pathway.<ref>PMID:11856323</ref>
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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/qz/1qzp_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=1qzp 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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Dematin (band 4.9) is found in the junctional complex of the spectrin cytoskeleton that supports the erythrocyte cell membrane. Dematin is a member of the larger class of cytoskeleton-associated proteins that contain a modular "headpiece" domain at their extreme C termini. The dematin headpiece domain provides the second F-actin-binding site required for in vitro F-actin bundling. The dematin headpiece is found in two forms in the cell, one of 68 residues (DHP) and one containing a 22-amino acid insert near its N terminus (DHP+22). In addition, dematin contains the only headpiece domain that is phosphorylated, in vivo. The 22-amino acid insert in DHP+22 appeared unstructured in NMR spectra; therefore, we have determined the three-dimensional structure of DHP by multidimensional NMR methods. Although the overall three-dimensional structure of DHP is similar to that of the villin headpiece, there are two novel characteristics revealed by this structure. First, unlike villin headpiece that contains a single buried salt bridge, DHP contains a buried charged cluster comprising residues Glu(39), Arg(66), Lys(70), and the C-terminal carboxylate of Phe(76). Second, (15)N relaxation experiments indicate that the longer "variable loop" region near the N terminus of DHP (residues 20-29) is dynamic, undergoing significantly greater motions that the rest of the structure. Furthermore, NMR chemical shift changes indicate that the conformation of the dynamic variable loop is altered by phosphorylation of serine 74, which is far in the sequence from the variable loop region. Our results suggest that phosphorylation of the dematin headpiece acts as a conformational switch within this headpiece domain.
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==Disease==
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The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site.,Frank BS, Vardar D, Chishti AH, McKnight CJ J Biol Chem. 2004 Feb 27;279(9):7909-16. Epub 2003 Dec 2. PMID:14660664<ref>PMID:14660664</ref>
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Known diseases associated with this structure: Amyotrophic lateral sclerosis, CHMP2B-related OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609512 609512]], Dementia, familial, nonspecific OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609512 609512]], XY sex reversal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602424 602424]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1QZP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QZP OCA].
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</div>
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<div class="pdbe-citations 1qzp" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site., Frank BS, Vardar D, Chishti AH, McKnight CJ, J Biol Chem. 2004 Feb 27;279(9):7909-16. Epub 2003 Dec 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14660664 14660664]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chishti, A.H.]]
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[[Category: Chishti AH]]
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[[Category: Frank, B.S.]]
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[[Category: Frank BS]]
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[[Category: McKnight, C.J.]]
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[[Category: McKnight CJ]]
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[[Category: Vardar, D.]]
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[[Category: Vardar D]]
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[[Category: actin binding domain]]
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[[Category: dematin headpiece]]
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[[Category: villin headpiece]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:57:52 2007''
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Current revision

NMR structure of the human dematin headpiece domain

PDB ID 1qzp

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