1ivt
From Proteopedia
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| - | [[Image:1ivt.gif|left|200px]] | + | [[Image:1ivt.gif|left|200px]] |
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| - | '''NMR structures of the C-terminal globular domain of human lamin A/C''' | + | {{Structure |
| + | |PDB= 1ivt |SIZE=350|CAPTION= <scene name='initialview01'>1ivt</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR structures of the C-terminal globular domain of human lamin A/C''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IVT is a [ | + | 1IVT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVT OCA]. |
==Reference== | ==Reference== | ||
| - | The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy., Krimm I, Ostlund C, Gilquin B, Couprie J, Hossenlopp P, Mornon JP, Bonne G, Courvalin JC, Worman HJ, Zinn-Justin S, Structure. 2002 Jun;10(6):811-23. PMID:[http:// | + | The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy., Krimm I, Ostlund C, Gilquin B, Couprie J, Hossenlopp P, Mornon JP, Bonne G, Courvalin JC, Worman HJ, Zinn-Justin S, Structure. 2002 Jun;10(6):811-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12057196 12057196] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ig-fold]] | [[Category: ig-fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:55:33 2008'' |
Revision as of 09:55, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structures of the C-terminal globular domain of human lamin A/C
Overview
Lamins are nuclear intermediate filaments that, together with lamin-associated proteins, maintain nuclear shape and provide a structural support for chromosomes and replicating DNA. We have determined the solution structure of the human lamin A/C C-terminal globular domain which contains specific mutations causing four different heritable diseases. This domain encompasses residues 430-545 and adopts an Ig-like fold of type s. We have also characterized by NMR and circular dichroism the structure and thermostability of three mutants, R453W and R482W/Q, corresponding to "hot spots" causing Emery-Dreifuss muscular dystrophy and Dunnigan-type lipodystrophy, respectively. Our structure determination and mutant analyses clearly show that the consequences of the mutations causing muscle-specific diseases or lipodystrophy are different at the molecular level.
About this Structure
1IVT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy., Krimm I, Ostlund C, Gilquin B, Couprie J, Hossenlopp P, Mornon JP, Bonne G, Courvalin JC, Worman HJ, Zinn-Justin S, Structure. 2002 Jun;10(6):811-23. PMID:12057196
Page seeded by OCA on Thu Mar 20 11:55:33 2008
