3umn

From Proteopedia

(Difference between revisions)

Revision as of 00:35, 5 August 2016

Crystal Structure of Lamin-B1

Structural highlights

3umn is a 3 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 3hn9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	LMNB1, LMN2, LMNB (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[LMNB1_HUMAN] Defects in LMNB1 are the cause of leukodystrophy demyelinating autosomal dominant adult-onset (ADLD) [MIM:169500]. ADLD is a slowly progressive and fatal demyelinating leukodystrophy, presenting in the fourth or fifth decade of life. Clinically characterized by early autonomic abnormalities, pyramidal and cerebellar dysfunction, and symmetric demyelination of the CNS. It differs from multiple sclerosis and other demyelinating disorders in that neuropathology shows preservation of oligodendroglia in the presence of subtotal demyelination and lack of astrogliosis.^[1]

Function

[LMNB1_HUMAN] Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.

Publication Abstract from PubMed

We present here the crystal structures of human lamin B1 globular tail domain and coiled 2B domain, which adopt similar folds to Ig-like domain and coiled-coil domain of lamin A, respectively. Despite the overall similarity, we found an extra intermolecular disulfide bond in the lamin B1 coil 2B domain, which does not exist in lamin A/C. In addition, the structural analysis indicates that interactions at the lamin B1 homodimer interface are quite different from those of lamin A/C. Thus our research not only reveals the diversely formed homodimers among lamin family members, but also sheds light on understanding the important roles of lamin B1 in forming the nuclear lamina matrix. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: Lamin-B and Lamin-Bbind by x-ray crystallography (View interaction).

Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1.,Ruan J, Xu C, Bian C, Lam R, Wang JP, Kania J, Min J, Zang J FEBS Lett. 2012 Feb 17;586(4):314-8. Epub 2012 Jan 16. PMID:22265972^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Padiath QS, Saigoh K, Schiffmann R, Asahara H, Yamada T, Koeppen A, Hogan K, Ptacek LJ, Fu YH. Lamin B1 duplications cause autosomal dominant leukodystrophy. Nat Genet. 2006 Oct;38(10):1114-23. Epub 2006 Sep 3. PMID:16951681 doi:ng1872
↑ Ruan J, Xu C, Bian C, Lam R, Wang JP, Kania J, Min J, Zang J. Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1. FEBS Lett. 2012 Feb 17;586(4):314-8. Epub 2012 Jan 16. PMID:22265972 doi:10.1016/j.febslet.2012.01.007

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3umn"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Lamin-B1==
 <StructureSection load='3umn' size='340' side='right' caption='[[3umn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3umn]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hn9 3hn9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UMN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3umn]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hn9 3hn9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UMN FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LMNB1, LMN2, LMNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LMNB1, LMN2, LMNB ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3umn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3umn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3umn RCSB], [http://www.ebi.ac.uk/pdbsum/3umn PDBsum]</span></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=3umn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3umn OCA], [http://pdbe.org/3umn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3umn RCSB], [http://www.ebi.ac.uk/pdbsum/3umn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3umn ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3umn" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Amaya, M F]]
 [[Category: Arrowsmith, C H]]

3umn

From Proteopedia

Revision as of 00:35, 5 August 2016

Crystal Structure of Lamin-B1

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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