SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation

Journal of Molecular Biology

Volumn 408, Issue 3, 2011, Pages 503-513

  Basaiawmoit, R V ^a   Oliveira, C L P ^b,e   Runager, K ^a   Sorensen C S ^a   Behrens, M A ^b   Jonsson, B H ^c   Kristensen, T ^a   Klintworth, G K ^d   Enghild, J J ^a   Pedersen, J Skov ^b   Otzen, D E ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b AARHUS UNIVERSITY   (Denmark)

^c LINKÖPING UNIVERSITY   (Sweden)

^d DUKE UNIVERSITY MEDICAL CENTER   (United States)

^e UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

ab initio modeling; corneal dystrophy; low resolution structure; oligomerization; rigid body fit

Indexed keywords

FASCICLIN I; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA INDUCED PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CORNEA DYSTROPHY; GENE; GENE MUTATION; GENETIC ASSOCIATION; HUMAN; HUMAN CELL; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; R124H GENE; ULTRACENTRIFUGATION; WILD TYPE; X RAY CRYSTALLOGRAPHY;

EID: 79953836704     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.02.052     Document Type: Article

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