1hmf: Difference between revisions

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 ==STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1==
-<StructureSection load='1hmf' size='340' side='right'caption='[[1hmf]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+<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/Buffalo_rat Buffalo rat]. 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>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hme|1hme]]</div></td></tr>
+</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).
+[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]]
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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=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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1hmf" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[High mobility group protein|High mobility group protein]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Hill, C S]]
+[[Category: Rattus norvegicus]]
-[[Category: Kraulis, P J]]
+[[Category: Hill CS]]
-[[Category: Laue, E D]]
+[[Category: Kraulis PJ]]
-[[Category: Raine, A R.C]]
+[[Category: Laue ED]]
-[[Category: Thomas, J O]]
+[[Category: Raine ARC]]
-[[Category: Weir, H M]]
+[[Category: Thomas JO]]
-[[Category: Dna-binding]]
+[[Category: Weir HM]]