1ghc

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{{Seed}}
 
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[[Image:1ghc.png|left|200px]]
 
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==HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5==
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The line below this paragraph, containing "STRUCTURE_1ghc", creates the "Structure Box" on the page.
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<StructureSection load='1ghc' size='340' side='right'caption='[[1ghc]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ghc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=1ghc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghc OCA], [https://pdbe.org/1ghc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghc RCSB], [https://www.ebi.ac.uk/pdbsum/1ghc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghc ProSAT]</span></td></tr>
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{{STRUCTURE_1ghc| PDB=1ghc | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/H11L_CHICK H11L_CHICK] Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.
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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/gh/1ghc_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=1ghc 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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The globular domain of chicken histone H1 (GH1) has been studied by 1H homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy. After the full assignment of the proton and 15N resonances, the tertiary structure of GH1 was determined by an iterative procedure using distance geometry and restrained simulated annealing. The secondary structure elements of GH1, three helices (S5-A16, S24-A34, N42-K56) followed by a beta-hairpin (L59-L73), are folded in a manner very similar to the corresponding parts of the globular domain of chicken histone H5 (GH5) [Clore et al. (1987) EMBO J. 6, 1833-1842; Ramakrishnan et al. (1993) Nature 362, 219-223]. However, subtle differences are detected between the two structures and between the electrostatic potentials surrounding the molecules. The most important differences are located in the loop between the second and third helices, a region that could be responsible for the different affinity for DNA. The most positively charged regions are not found in exactly the same position in GH1 and GH5. Nevertheless, their location seems to agree with the model where nucleosome binding takes place through contact points located at one DNA terminus and close to the dyad axis of the nucleosome [Schwabe &amp; Travers (1993) Curr. Biol. 3, 628-630].
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===HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5===
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Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5.,Cerf C, Lippens G, Ramakrishnan V, Muyldermans S, Segers A, Wyns L, Wodak SJ, Hallenga K Biochemistry. 1994 Sep 20;33(37):11079-86. PMID:7727360<ref>PMID:7727360</ref>
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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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<div class="pdbe-citations 1ghc" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_7727360}}, adds the Publication Abstract to the page
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*[[Histone 3D structures|Histone 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 7727360 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_7727360}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1GHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHC OCA].
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==Reference==
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Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5., Cerf C, Lippens G, Ramakrishnan V, Muyldermans S, Segers A, Wyns L, Wodak SJ, Hallenga K, Biochemistry. 1994 Sep 20;33(37):11079-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7727360 7727360]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cerf, C.]]
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[[Category: Cerf C]]
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[[Category: Hallenga, K.]]
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[[Category: Hallenga K]]
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[[Category: Lippens, G.]]
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[[Category: Lippens G]]
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[[Category: Muyldermans, S.]]
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[[Category: Muyldermans S]]
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[[Category: Ramakrishnan, V.]]
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[[Category: Ramakrishnan V]]
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[[Category: Segers, A.]]
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[[Category: Segers A]]
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[[Category: Wodak, S J.]]
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[[Category: Wodak SJ]]
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[[Category: Wyns, L.]]
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[[Category: Wyns L]]
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[[Category: Chromosomal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:17:13 2008''
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Current revision

HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5

PDB ID 1ghc

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