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Literature summary for 2.7.10.1 extracted from

  • Chao, K.L.; Tsai, I.W.; Chen, C.; Herzberg, O.
    Crystal structure of the Sema-PSI extracellular domain of human RON receptor tyrosine kinase (2012), PLoS ONE, 7, e41912.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of semaphorin/plexins-semaphorins-integrins domains at 1.85 A resolution. The semaphorin domain adopts a sevenbladed beta-propeller fold, followed by disulfide bond rich, cysteine-knot plexins-semaphorins-integrins motif. the semaphorin/plexins-semaphorins-integrins domains define the receptors’ exclusive selectivity towards their respective ligands. The crystal packing generates a homodimer with interface formed by the semaphorin domain. The dimer interface overlaps with the putative macrophage stimulating protein-b binding site Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Homo sapiens Q04912 macrophage-stimulating protein receptor
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Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
macrophage-stimulating protein receptor
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Homo sapiens
Recepteur d’Origine Nantais
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Homo sapiens
RON receptor tyrosine kinase
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Homo sapiens