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| | <StructureSection load='2bzf' size='340' side='right'caption='[[2bzf]], [[Resolution|resolution]] 2.87Å' scene=''> | | <StructureSection load='2bzf' size='340' side='right'caption='[[2bzf]], [[Resolution|resolution]] 2.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bzf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bzf]] is a 3 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=2BZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZF 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;'>[[1ci4|1ci4]], [[1qck|1qck]], [[2ezx|2ezx]], [[2ezy|2ezy]], [[2ezz|2ezz]]</div></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]] 2.87Å</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=2bzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bzf OCA], [https://pdbe.org/2bzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bzf RCSB], [https://www.ebi.ac.uk/pdbsum/2bzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bzf 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=2bzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bzf OCA], [https://pdbe.org/2bzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bzf RCSB], [https://www.ebi.ac.uk/pdbsum/2bzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bzf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[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>
| + | [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 == |
| - | [[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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bradley, C M]] | + | [[Category: Bradley CM]] |
| - | [[Category: Craigie, R]] | + | [[Category: Craigie R]] |
| - | [[Category: Dyda, F]] | + | [[Category: Dyda F]] |
| - | [[Category: Ghirlando, R]] | + | [[Category: Ghirlando R]] |
| - | [[Category: Ronning, D R]] | + | [[Category: Ronning DR]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna compaction]]
| + | |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Lem family]]
| + | |
| - | [[Category: Non-specific dna-binding]]
| + | |
| - | [[Category: Nuclear organization]]
| + | |
| - | [[Category: Retroviral integration]]
| + | |
| 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]
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 ability of barrier-to-autointegration factor (BAF) to bind and bridge DNA in a sequence-independent manner is crucial for its role in retroviral integration and a variety of cellular processes. To better understand this behavior, we solved the crystal structure of BAF bound to DNA. The structure reveals that BAF bridges DNA using two pairs of helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer without changing its conformation.
Structural basis for DNA bridging by barrier-to-autointegration factor.,Bradley CM, Ronning DR, Ghirlando R, Craigie R, Dyda F Nat Struct Mol Biol. 2005 Oct;12(10):935-6. Epub 2005 Sep 11. PMID:16155580[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Bradley CM, Ronning DR, Ghirlando R, Craigie R, Dyda F. Structural basis for DNA bridging by barrier-to-autointegration factor. Nat Struct Mol Biol. 2005 Oct;12(10):935-6. Epub 2005 Sep 11. PMID:16155580 doi:10.1038/nsmb989
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