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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2010-10-7
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pubmed:abstractText |
Members of the TGF-? superfamily are characterized by a highly promiscuous ligand-receptor interaction as is readily apparent from the numeral discrepancy of only seven type I and five type II receptors available for more than 40 ligands. Structural and functional studies have been used to address the question of how specific signals can be deduced from a limited number of receptor combinations and to unravel the molecular mechanisms underlying the protein-protein recognition that allow such limited specificity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:meshHeading |
pubmed-meshheading:20927405-Animals,
pubmed-meshheading:20927405-Bone Morphogenetic Protein 2,
pubmed-meshheading:20927405-Bone Morphogenetic Protein Receptors, Type I,
pubmed-meshheading:20927405-Cell Line,
pubmed-meshheading:20927405-Crystallography, X-Ray,
pubmed-meshheading:20927405-Humans,
pubmed-meshheading:20927405-Immunoglobulin Fab Fragments,
pubmed-meshheading:20927405-Ligands,
pubmed-meshheading:20927405-Mice,
pubmed-meshheading:20927405-Models, Molecular,
pubmed-meshheading:20927405-Molecular Conformation,
pubmed-meshheading:20927405-Protein Binding,
pubmed-meshheading:20927405-Protein Structure, Tertiary
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pubmed:year |
2010
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pubmed:articleTitle |
A selection fit mechanism in BMP receptor IA as a possible source for BMP ligand-receptor promiscuity.
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pubmed:affiliation |
Lehrstuhl für Physiologische Chemie II, Theodor-Boveri-Institut für Biowissenschaften der Universität Würzburg, Würzburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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