The sema domain

Current Opinion in Structural Biology

Volumn 14, Issue 6, 2004, Pages 669-678

  Gherardi, Ermanno ^a   Love, Christopher A ^b   Esnouf, Robert M ^b   Jones, E Yvonne ^b  

^a MEDICAL RESEARCH COUNCIL   (United Kingdom)

^b Division of Structural Biology   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE; SEMAPHORIN; SEMAPHORIN 3A;

ADAPTATION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; BIOCHEMISTRY; CANCER; CARBOXY TERMINAL SEQUENCE; CELL MIGRATION; CELLULAR DISTRIBUTION; CRYSTAL STRUCTURE; DELETION MUTANT; GENETICS; MUTAGENESIS; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SEQUENCE ANALYSIS; TRANSCRIPTION INITIATION;

ANIMALS; BINDING SITES; HUMANS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR PROTEIN-TYROSINE KINASES; SEMAPHORINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 9944258621     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.10.010     Document Type: Review

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34. ••], this provides the first structural data on the sema domain, revealing the β-propeller topology. By combining their structural and functional data, the authors define a putative binding site for the neuropilin 1 receptor on the top face of the sema domain.
35. ••]).
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45. D. Angeloni, A. Danilkovitch-Miagkova, A. Miagkov, E.J. Leonard, and M.I. Lerman The soluble sema domain of the RON receptor inhibits macrophage-stimulating protein-induced receptor activation J Biol Chem 279 2004 3726 3732 This study defines a role in ligand binding for the sema domain of the RON receptor by demonstrating that a soluble form of the sema domain inhibits both binding of HGFl/MSP to native RON and receptor signalling.
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48. A.M. Koppel, L. Feiner, H. Kobayashi, and J.A. Raper A 70 amino acid region within the semaphorin domain activates specific cellular response of semaphorin family members Neuron 19 1997 531 537
49. M. Kong-Beltran, J. Stamos, and D. Wickramasinghe The Sema domain of Met is necessary for receptor dimerization and activation Cancer Cell 6 2004 75 84 This mutagenesis and biochemical study provides valuable confirmation of the role of the sema domain of MET in ligand binding and demonstrates receptor dimerisation following ligand binding. The study also establishes that a soluble form of MET comprising the sema domain and CRD inhibits the migratory cell response to HGF/SF.
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