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1dz7

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(New page: 200px<br /> <applet load="1dz7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dz7" /> '''SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMA...)
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[[Image:1dz7.gif|left|200px]]<br />
 
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<applet load="1dz7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dz7" />
 
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'''SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMAN CHORIONIC GONADOTROPIN [MODELED WITHOUT CARBOHYDRATE RESIDUES]'''<br />
 
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==Overview==
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==Solution structure of the a-subunit of human chorionic gonadotropin [modeled without carbohydrate residues]==
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The three-dimensional solution structure of the alpha-subunit in the, alpha, beta heterodimeric human chorionic gonadotropin (hCG), deglycosylated with endo-beta-N-acetylglucosaminidase-B (dg-alpha hCG), was determined using 2D homonuclear and 2D heteronuclear 1H, 13C NMR, spectroscopy at natural abundance in conjunction with the program package, XPLOR. The distance geometry/simulated annealing protocol was modified to, allow for the efficient modelling of the cystine knot motif present in, alpha hCG. The protein structure was modelled with 620 interproton, distance restraints and the GlcNAc residue linked to Asn78 was modelled, with 30 protein-carbohydrate and 3 intraresidual NOEs. The solution, structure of dg-alpha hCG is represented by an ensemble of 27 structures., In comparison to the crystal structure of the dimer, the solution, structure of free dg-alpha hCG exhibits: (a) an increased structural, disorder (residues 33-57); (b) a different backbone conformation near, Val76 and Glu77; and (c) a larger flexibility. These differences are, caused by the absence of the interactions with the beta-subunit., Consequently, in free dg-alpha hCG, compared to the intact dimer, the two, hairpin loops 20-23 and 70-74 are arranged differently with respect to, each other. The beta-GlcNAc(78) is tightly associated with the hydrophobic, protein-core in between the beta-hairpins. This conclusion is based on the, NOEs from the axial H1, H3, H5 atoms and the N-acetyl protons of, beta-GlcNAc(78) to the protein-core. The hydrophobic protein-core between, the beta-hairpins is thereby shielded from the solvent.
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<StructureSection load='1dz7' size='340' side='right'caption='[[1dz7]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dz7]] 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=1DZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZ7 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=1dz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz7 OCA], [https://pdbe.org/1dz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dz7 RCSB], [https://www.ebi.ac.uk/pdbsum/1dz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLHA_HUMAN GLHA_HUMAN]
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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/dz/1dz7_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=1dz7 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DZ7 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=1DZ7 OCA].
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*[[Hormone|Hormone]]
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__TOC__
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==Reference==
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</StructureSection>
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Solution structure of the alpha-subunit of human chorionic gonadotropin., Erbel PJ, Karimi-Nejad Y, De Beer T, Boelens R, Kamerling JP, Vliegenthart JF, Eur J Biochem. 1999 Mar;260(2):490-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10095786 10095786]
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[[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: Beer, T.De.]]
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[[Category: Boelens R]]
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[[Category: Boelens, R.]]
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[[Category: De Beer T]]
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[[Category: Erbel, P.J.A.]]
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[[Category: Erbel PJA]]
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[[Category: Kamerling, J.P.]]
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[[Category: Kamerling JP]]
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[[Category: Karimi-Nejad, Y.]]
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[[Category: Karimi-Nejad Y]]
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[[Category: Vliegenthart, J.F.G.]]
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[[Category: Vliegenthart JFG]]
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[[Category: chorionic gonadotropin]]
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[[Category: chorionic gonadotropin free a subunit]]
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[[Category: cystine knot]]
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[[Category: glycoprotein structure]]
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[[Category: nmr]]
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[[Category: xplor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:37:35 2007''
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Current revision

Solution structure of the a-subunit of human chorionic gonadotropin [modeled without carbohydrate residues]

PDB ID 1dz7

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