ArticleProtein science : a publication of the Protein Society2006
NMR structure of the first Ig module of mouse FGFR1.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 18 citations in OpenAlex.
- Isoform-specific inhibition of FGFR signaling achieved by a de-novo-designed mini-protein.Cell reports · 2022Article
- Unliganded fibroblast growth factor receptor 1 forms density-independent dimers.The Journal of biological chemistry · 2015Article
- Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology.Cold Spring Harbor perspectives in biology · 2013Review
- The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition.Structure (London, England : 1993) · 2012Article
- Influence of heparin mimetics on assembly of the FGF.FGFR4 signaling complex.The Journal of biological chemistry · 2010Article
- Impaired fibroblast growth factor receptor 1 signaling as a cause of normosmic idiopathic hypogonadotropic hypogonadism.The Journal of clinical endocrinology and metabolism · 2009Article
- Structural basis for the activation of FGFR by NCAM.Protein science : a publication of the Protein Society · 2008Article
- Impaired FGF signaling contributes to cleft lip and palate.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Elucidation of the mechanism of the regulatory function of the Ig1 module of the fibroblast growth factor receptor 1.Protein science : a publication of the Protein Society · 2006Article
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4 authors.
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Abstract
Fibroblast growth factor (FGF) receptors (FGFRs) regulate a multitude of cellular processes during embryogenesis and in the adult. The extracellular part of the prototypical FGFR consists of three Ig modules (Ig1 - Ig3), in which Ig2 and Ig3 determine affinity and specificity for FGF and heparin, while the Ig1 module is thought to have a regulatory function. The crystal structures of the Ig2 and Ig3 modules alone and in complex with FGF have previously been reported. The structure of the Ig1 module is unknown, and very little is known about the structural determinants for the regulatory function of this module. We describe here the NMR structure of the Ig1 module of mouse FGFR1. The three-dimensional fold of the module belongs to the intermediate Ig subgroup and can be described as a beta-barrel consisting of two beta-sheets. One sheet is formed by A', G, F, C, and C', and the other by A, B, B', E, and D beta-strands. The overall strand topology of the Ig1 module is similar to that of the Ig2 and Ig3 modules. However, the A/A' loop of the Ig1 module is much longer than that of the Ig2 and Ig3 modules. It contains eight extra residues compared to the Ig3 module, and five extra residues compared to Ig2.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.