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SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation.
MedLine Citation:
PMID:  21371477     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Human transforming growth factor beta induced protein (TGFBIp) is composed of 683 residues including an N-terminal cysteine-rich (EMI) domain, four homologous fasciclin domains and an Arg-Gly-Asp (RGD) motif near the C-terminal. The protein is of interest because mutations in the TGFBI gene encoding TGFBIp lead to corneal dystrophies, a condition where protein aggregates within the cornea compromise transparency. The complete three-dimensional structure of TGFBIp is not yet available, with the exception of a partial X-ray structure of the archetype FAS1 domain derived from Drosophila fasciclin-1. In this study, small-angle x-ray scattering (SAXS) models of intact wild type human TGFBIp and a mutant (R124H) are presented. The mutation R124H leads to a variant of granular corneal dystrophy. The deduced structure of the TGFBIp monomer consists of four FAS1 domains in a simple "beads-on-a-string" arrangement, constructed by the superimposition of four consecutive Drosophila fasciclin domains. The SAXS-based model of the TGFBIp R124H mutant displayed no structural differences compared to the wild type. Both wild type TGFBIp and the R124H mutant formed trimers at higher protein concentrations. The similar association properties and three-dimensional shape of the two proteins suggest that the mutation does not induce any major structural rearrangements but points towards the role of other corneal specific factors in the formation of the corneal R124H deposits.
Authors:
R V Basaiawmoit; C L P Oliveira; K Runager; C S Sørensen; M A Behrens; B-H Jonsson; T Kristensen; G K Klintworth; J J Enghild; J Skov Pedersen; D E Otzen
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-2-28
Journal Detail:
Title:  Journal of molecular biology     Volume:  -     ISSN:  1089-8638     ISO Abbreviation:  -     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-3-4     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011. Published by Elsevier Ltd.
Affiliation:
Center for Insoluble Protein Structures (inSPIN), iNANO Interdisciplinary Nanoscience Center, Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark.
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