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  • The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D

    Author(s)
    Love, CA
    Harlos, K
    Mavaddat, N
    Davis, SJ
    Stuart, DI
    Jones, EY
    Esnouf, RM
    Griffith University Author(s)
    Love, Christopher A.
    Year published
    2003
    Metadata
    Show full item record
    Abstract
    Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal structure of SEMA4D (residues 1-657) shows the sema topology to be a seven-bladed beta-propeller, revealing an unexpected homology with integrins. The sema beta-propeller contains a distinctive 77-residue insertion between beta-strands C and D of blade 5. Blade 7 is followed by a domain common to plexins, semaphorins and integrins (PSI domain), which forms a compact cysteine knot abutting the side of the propeller, and an Ig-like domain. The top face of the beta-propeller presents prominent ...
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    Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal structure of SEMA4D (residues 1-657) shows the sema topology to be a seven-bladed beta-propeller, revealing an unexpected homology with integrins. The sema beta-propeller contains a distinctive 77-residue insertion between beta-strands C and D of blade 5. Blade 7 is followed by a domain common to plexins, semaphorins and integrins (PSI domain), which forms a compact cysteine knot abutting the side of the propeller, and an Ig-like domain. The top face of the beta-propeller presents prominent loops characteristic of semaphorins. In addition to limited contact between the Ig-like domains, the homodimer is stabilized through extensive interactions between the top faces in a sector of the beta-propeller used for heterodimerization in integrins. This face of the propeller also mediates ligand binding in integrins, and functional data for semaphorin-receptor interactions map to the equivalent surface.
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    Journal Title
    Nature Structural Biology
    Volume
    10
    Issue
    10
    Publisher URI
    http://www.nature.com/nsmb/index.html
    DOI
    https://doi.org/10.1038/nsb977
    Copyright Statement
    © 2003 Nature Publishing Group. Please refer to the journal's website for access to the definitive, published version.
    Subject
    Chemical sciences
    Biological sciences
    Biomedical and clinical sciences
    Publication URI
    http://hdl.handle.net/10072/16925
    Collection
    • Journal articles

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