1ifr: Difference between revisions

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[[Image:1ifr.jpg|left|200px]]
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{{STRUCTURE_1ifr|  PDB=1ifr  |  SCENE=  }}  
{{STRUCTURE_1ifr|  PDB=1ifr  |  SCENE=  }}  


'''Structure of Lamin A/C Globular Domain'''
===Structure of Lamin A/C Globular Domain===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11901143}}


==About this Structure==
==About this Structure==
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[[Category: Werner, E D.]]
[[Category: Werner, E D.]]
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
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Revision as of 07:53, 1 July 2008

File:1ifr.png

Template:STRUCTURE 1ifr

Structure of Lamin A/C Globular Domain

Template:ABSTRACT PUBMED 11901143

About this Structure

1IFR is a Single protein structure of sequence from Homo sapiens. 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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