1ifr
From Proteopedia
(New page: 200px<br /><applet load="1ifr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ifr, resolution 1.4Å" /> '''Structure of Lamin A/...) |
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| - | [[Image:1ifr.jpg|left|200px]]<br /><applet load="1ifr" size=" | + | [[Image:1ifr.jpg|left|200px]]<br /><applet load="1ifr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ifr, resolution 1.4Å" /> | caption="1ifr, resolution 1.4Å" /> | ||
'''Structure of Lamin A/C Globular Domain'''<br /> | '''Structure of Lamin A/C Globular Domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The nuclear lamins form a two-dimensional matrix that provides integrity | + | The nuclear lamins form a two-dimensional matrix that provides integrity to the cell nucleus and participates in nuclear activities. Mutations in the region of human LMNA encoding the carboxyl-terminal tail Lamin A/C are associated with forms of muscular dystrophy and familial partial lipodystrophy (FPLD). To help discriminate tissue-specific phenotypes, we have solved at 1.4-A resolution the three-dimensional crystal structure of the lamin A/C globular tail. The domain adopts a novel, all beta immunoglobulin-like fold. FPLD-associated mutations cluster within a small surface, whereas muscular dystrophy-associated mutations are distributed throughout the protein core and on its surface. These findings distinguish myopathy- and lipodystrophy-associated mutations and provide a structural framework for further testing hypotheses concerning lamin function. |
==About this Structure== | ==About this Structure== | ||
| - | 1IFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dhe-Paganon, S.]] | [[Category: Dhe-Paganon, S.]] | ||
| - | [[Category: Shoelson, S | + | [[Category: Shoelson, S E.]] |
| - | [[Category: Werner, E | + | [[Category: Werner, E D.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:27 2008'' |
Revision as of 11:11, 21 February 2008
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Structure of Lamin A/C Globular Domain
Overview
The nuclear lamins form a two-dimensional matrix that provides integrity to the cell nucleus and participates in nuclear activities. Mutations in the region of human LMNA encoding the carboxyl-terminal tail Lamin A/C are associated with forms of muscular dystrophy and familial partial lipodystrophy (FPLD). To help discriminate tissue-specific phenotypes, we have solved at 1.4-A resolution the three-dimensional crystal structure of the lamin A/C globular tail. The domain adopts a novel, all beta immunoglobulin-like fold. FPLD-associated mutations cluster within a small surface, whereas muscular dystrophy-associated mutations are distributed throughout the protein core and on its surface. These findings distinguish myopathy- and lipodystrophy-associated mutations and provide a structural framework for further testing hypotheses concerning lamin function.
About this Structure
1IFR is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the globular tail of nuclear lamin., Dhe-Paganon S, Werner ED, Chi YI, Shoelson SE, J Biol Chem. 2002 May 17;277(20):17381-4. Epub 2002 Mar 18. PMID:11901143
Page seeded by OCA on Thu Feb 21 13:11:27 2008
