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| | <StructureSection load='6unt' size='340' side='right'caption='[[6unt]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6unt' size='340' side='right'caption='[[6unt]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6unt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UNT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UNT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6unt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UNT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ci4|1ci4]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BANF1, BAF, BCRG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6unt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6unt OCA], [https://pdbe.org/6unt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6unt RCSB], [https://www.ebi.ac.uk/pdbsum/6unt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6unt ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6unt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6unt OCA], [http://pdbe.org/6unt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6unt RCSB], [http://www.ebi.ac.uk/pdbsum/6unt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6unt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/BAF_HUMAN BAF_HUMAN]] Defects in BANF1 are the cause of Nestor-Guillermo progeria syndrome (NGPS) [MIM:[http://omim.org/entry/614008 614008]]. NGPS is an atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognatia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.<ref>PMID:21549337</ref> | + | [https://www.uniprot.org/uniprot/BAF_HUMAN BAF_HUMAN] Defects in BANF1 are the cause of Nestor-Guillermo progeria syndrome (NGPS) [MIM:[https://omim.org/entry/614008 614008]. NGPS is an atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognatia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.<ref>PMID:21549337</ref> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BAF_HUMAN BAF_HUMAN]] Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.<ref>PMID:11005805</ref> <ref>PMID:12163470</ref> <ref>PMID:16680152</ref> | + | [https://www.uniprot.org/uniprot/BAF_HUMAN BAF_HUMAN] Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.<ref>PMID:11005805</ref> <ref>PMID:12163470</ref> <ref>PMID:16680152</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The multiple-solvent crystal structure (MSCS) approach uses high concentrations of organic solvents to characterize the interactions and effects of solvents on proteins. Here, the method has been further developed and an MSCS data-handling pipeline is presented that uses the Detection of Related Solvent Positions (DRoP) program to improve data quality. DRoP is used to selectively model conserved water molecules, so that an advanced stage of structural refinement is reached quickly. This allows the placement of organic molecules more accurately and convergence on high-quality maps and structures. This pipeline was applied to the chromatin-associated protein barrier-to-autointegration factor (BAF), resulting in structural models with better than average statistics. DRoP and Phenix Structure Comparison were used to characterize the data sets and to identify a binding site that overlaps with the interaction site of BAF with emerin. The conserved water-mediated networks identified by DRoP suggested a mechanism by which water molecules are used to drive the binding of DNA. Normalized and differential B-factor analysis is shown to be a valuable tool to characterize the effects of specific solvents on defined regions of BAF. Specific solvents are identified that cause stabilization of functionally important regions of the protein. This work presents tools and a standardized approach for the analysis and comprehension of MSCS data sets.
| + | |
| - | | + | |
| - | Development of a structure-analysis pipeline using multiple-solvent crystal structures of barrier-to-autointegration factor.,Agarwal S, Smith M, De La Rosa I, Verba KA, Swartz P, Segura-Totten M, Mattos C Acta Crystallogr D Struct Biol. 2020 Oct 1;76(Pt 10):1001-1014. doi:, 10.1107/S2059798320011341. Epub 2020 Sep 17. PMID:33021502<ref>PMID:33021502</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6unt" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Agarwal, S]] | + | [[Category: Agarwal S]] |
| - | [[Category: Kliment, A V]] | + | [[Category: De La Rosa I]] |
| - | [[Category: Mattos, C]] | + | [[Category: Kliment AV]] |
| - | [[Category: Rosa, I De La]] | + | [[Category: Mattos C]] |
| - | [[Category: Segura-Totten, M]] | + | [[Category: Segura-Totten M]] |
| - | [[Category: Smith, M]] | + | [[Category: Smith M]] |
| - | [[Category: Swartz, P]] | + | [[Category: Swartz P]] |
| - | [[Category: Alpha helical]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Minor groove binder]]
| + | |
| - | [[Category: Msc]]
| + | |
| Structural highlights
Disease
BAF_HUMAN Defects in BANF1 are the cause of Nestor-Guillermo progeria syndrome (NGPS) [MIM:614008. NGPS is an atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognatia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.[1]
Function
BAF_HUMAN Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.[2] [3] [4]
References
- ↑ Puente XS, Quesada V, Osorio FG, Cabanillas R, Cadinanos J, Fraile JM, Ordonez GR, Puente DA, Gutierrez-Fernandez A, Fanjul-Fernandez M, Levy N, Freije JM, Lopez-Otin C. Exome sequencing and functional analysis identifies BANF1 mutation as the cause of a hereditary progeroid syndrome. Am J Hum Genet. 2011 May 13;88(5):650-6. doi: 10.1016/j.ajhg.2011.04.010. Epub, 2011 May 5. PMID:21549337 doi:10.1016/j.ajhg.2011.04.010
- ↑ Harris D, Engelman A. Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro. J Biol Chem. 2000 Dec 15;275(50):39671-7. PMID:11005805 doi:10.1074/jbc.M002626200
- ↑ Segura-Totten M, Kowalski AK, Craigie R, Wilson KL. Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J Cell Biol. 2002 Aug 5;158(3):475-85. Epub 2002 Aug 5. PMID:12163470 doi:10.1083/jcb.200202019
- ↑ Jacque JM, Stevenson M. The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity. Nature. 2006 Jun 1;441(7093):641-5. Epub 2006 May 7. PMID:16680152 doi:10.1038/nature04682
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