1ifr
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(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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Revision as of 15:15, 20 November 2007
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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 GOL 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
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