|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==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]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1hmf' size='340' side='right'caption='[[1hmf]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hmf]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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">[[1hme|1hme]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmf OCA], [http://pdbe.org/1hmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hmf RCSB], [http://www.ebi.ac.uk/pdbsum/1hmf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmf ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 28: |
Line 28: |
| | </div> | | </div> |
| | <div class="pdbe-citations 1hmf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1hmf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[High mobility group protein|High mobility group protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </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]] |
| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weir HM, Kraulis PJ, Hill CS, Raine AR, Laue ED, Thomas JO. Structure of the HMG box motif in the B-domain of HMG1. EMBO J. 1993 Apr;12(4):1311-9. PMID:8467791
|
