1ivt
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(New page: 200px<br /><applet load="1ivt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ivt" /> '''NMR structures of the C-terminal globular do...)
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Revision as of 15:35, 20 November 2007
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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
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