2ezz

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Revision as of 17:03, 15 January 2015

SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES

Structural highlights

2ezz is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

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 solution structure of the human barrier-to-autointegration factor, BAF, a 21,000 Mr dimer, has been solved by NMR, including extensive use of dipolar couplings which provide a priori long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3-5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.

Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration.,Cai M, Huang Y, Zheng R, Wei SQ, Ghirlando R, Lee MS, Craigie R, Gronenborn AM, Clore GM Nat Struct Biol. 1998 Oct;5(10):903-9. PMID:9783751^[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
↑ Cai M, Huang Y, Zheng R, Wei SQ, Ghirlando R, Lee MS, Craigie R, Gronenborn AM, Clore GM. Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration. Nat Struct Biol. 1998 Oct;5(10):903-9. PMID:9783751 doi:http://dx.doi.org/10.1038/2345

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ezz"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2ezz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EZZ FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ezz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ezz RCSB], [http://www.ebi.ac.uk/pdbsum/2ezz PDBsum]</span></td></tr>
+</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=2ezz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ezz RCSB], [http://www.ebi.ac.uk/pdbsum/2ezz PDBsum]</span></td></tr>
-<table>
+</table>
 == 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>
@@ Line 32: / Line 32: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Cai, M.]]
+[[Category: Cai, M]]
-[[Category: Clore, G M.]]
+[[Category: Clore, G M]]
-[[Category: Gronenborn, A M.]]
+[[Category: Gronenborn, A M]]
 [[Category: Aid]]
 [[Category: Dna-binding protein]]
 [[Category: Integration]]
 [[Category: Retroviruse]]

2ezz

From Proteopedia

Revision as of 17:03, 15 January 2015

SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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