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[[Image:1hmf.gif|left|200px]]
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{{STRUCTURE_1hmf|  PDB=1hmf  |  SCENE=  }}
'''STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1'''


==STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1==
<StructureSection load='1hmf' size='340' side='right'caption='[[1hmf]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hmf]] 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=1HMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmf OCA], [https://pdbe.org/1hmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmf RCSB], [https://www.ebi.ac.uk/pdbsum/1hmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmf ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/1hmf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1hmf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMF OCA].
</div>
<div class="pdbe-citations 1hmf" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/8467791 8467791]
*[[High mobility group protein|High mobility group protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Hill CS]]
[[Category: Hill, C S.]]
[[Category: Kraulis PJ]]
[[Category: Kraulis, P J.]]
[[Category: Laue ED]]
[[Category: Laue, E D.]]
[[Category: Raine ARC]]
[[Category: Raine, A R.C.]]
[[Category: Thomas JO]]
[[Category: Thomas, J O.]]
[[Category: Weir HM]]
[[Category: Weir, H M.]]
[[Category: Dna-binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:00:55 2008''
Retrieved from "https://proteopedia.org/1hmf"