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dc.contributor.authorLove, CA
dc.contributor.authorHarlos, K
dc.contributor.authorMavaddat, N
dc.contributor.authorDavis, SJ
dc.contributor.authorStuart, DI
dc.contributor.authorJones, EY
dc.contributor.authorEsnouf, RM
dc.date.accessioned2017-05-03T11:37:23Z
dc.date.available2017-05-03T11:37:23Z
dc.date.issued2003
dc.date.modified2009-09-03T07:14:39Z
dc.identifier.issn1072-8368
dc.identifier.doi10.1038/nsb977
dc.identifier.urihttp://hdl.handle.net/10072/16925
dc.description.abstractSemaphorins, 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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoen_AU
dc.publisherNature Publishing Group
dc.publisher.placeUnited States
dc.publisher.urihttp://www.nature.com/nsmb/index.html
dc.relation.ispartofpagefrom843
dc.relation.ispartofpageto848
dc.relation.ispartofissue10
dc.relation.ispartofjournalNature Structural Biology
dc.relation.ispartofvolume10
dc.subject.fieldofresearchChemical Sciences
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode03
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.titleThe ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2003 Nature Publishing Group. Please refer to the journal's website for access to the definitive, published version.
gro.date.issued2003
gro.hasfulltextNo Full Text
gro.griffith.authorLove, Christopher A.


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