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1hme

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{{Seed}}
 
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[[Image:1hme.png|left|200px]]
 
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==STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1==
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The line below this paragraph, containing "STRUCTURE_1hme", creates the "Structure Box" on the page.
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<StructureSection load='1hme' size='340' side='right'caption='[[1hme]]' 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'>[[1hme]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HME 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=1hme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hme OCA], [https://pdbe.org/1hme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hme RCSB], [https://www.ebi.ac.uk/pdbsum/1hme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hme ProSAT]</span></td></tr>
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{{STRUCTURE_1hme| PDB=1hme | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HMGB1_RAT HMGB1_RAT] DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity).
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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/hm/1hme_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=1hme 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 conserved, abundant chromosomal protein HMG1 consists of two highly homologous, folded, basic DNA-binding domains, each of approximately 80 amino acid residues, and an acidic C-terminal tail. Each folded domain represents an 'HMG box', a sequence motif recently recognized in certain sequence-specific DNA-binding proteins and which also occurs in abundant HMG1-like proteins that bind to DNA without sequence specificity. The HMG box is defined by a set of highly conserved residues (most distinctively aromatic and basic) and appears to define a novel DNA-binding structural motif. We have expressed the HMG box region of the B-domain of rat HMG1 (residues 88-164 of the intact protein) in Escherichia coli and we describe here the determination of its structure by 2D 1H-NMR spectroscopy. There are three alpha-helices (residues 13-29, 34-48 and 50-74), which together account for approximately 75% of the total residues and contain many of the conserved basic and aromatic residues. Strikingly, the molecule is L-shaped, the angle of approximately 80 degrees between the two arms being defined by a cluster of conserved, predominantly aromatic, residues. The distinctive shape of the HMG box motif, which is distinct from hitherto characterized DNA-binding motifs, may be significant in relation to its recognition of four-way DNA junctions.
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===STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1===
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Structure of the HMG box motif in the B-domain of HMG1.,Weir HM, Kraulis PJ, Hill CS, Raine AR, Laue ED, Thomas JO EMBO J. 1993 Apr;12(4):1311-9. PMID:8467791<ref>PMID:8467791</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 1hme" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8467791}}, adds the Publication Abstract to the page
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*[[High mobility group protein|High mobility group protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8467791 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8467791}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1HME is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HME OCA].
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==Reference==
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<ref group="xtra">PMID:8467791</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Hill, C S.]]
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[[Category: Hill CS]]
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[[Category: Kraulis, P J.]]
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[[Category: Kraulis PJ]]
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[[Category: Laue, E D.]]
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[[Category: Laue ED]]
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[[Category: Raine, A R.C.]]
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[[Category: Raine ARC]]
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[[Category: Thomas, J O.]]
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[[Category: Thomas JO]]
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[[Category: Weir, H M.]]
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[[Category: Weir HM]]
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[[Category: Dna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:01:37 2009''
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Current revision

STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1

PDB ID 1hme

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