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dc.contributor.authorGherardi, E
dc.contributor.authorLove, CA
dc.contributor.authorEsnouf, RM
dc.contributor.authorJones, EY
dc.date.accessioned2017-05-03T11:37:23Z
dc.date.available2017-05-03T11:37:23Z
dc.date.issued2004
dc.date.modified2009-09-03T07:16:58Z
dc.identifier.issn0959-440X
dc.identifier.doi10.1016/j.sbi.2004.10.010
dc.identifier.urihttp://hdl.handle.net/10072/16923
dc.description.abstractThe sema domain was first defined from sequence by Kolodkin and colleagues in the early 1990s, and constitutes the distinctive structural and functional element of semaphorins, their plexin receptors and the receptor tyrosine kinases MET and RON, three protein families with major roles in development, tissue regeneration and cancer. Recently determined crystal structures of two semaphorins (SEMA3A and SEMA4D) and the MET receptor have shown that the sema domain consists of a highly conserved variant form of the seven-blade beta-propeller fold. The structures, however, also suggest differences between these families with respect to the mode of dimerisation and the regions of the domain involved in ligand-receptor interactions. This reflects the considerable plasticity and adaptation of the sema domain in order to meet different binding requirements, properties that may underlie the vast array of ligand-receptor specificities and functions of the semaphorin superfamily.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeUnited Kingdom
dc.publisher.urihttp://www.sciencedirect.com/science/journal/0959440X
dc.relation.ispartofpagefrom669
dc.relation.ispartofpageto678
dc.relation.ispartofjournalCurrent Opinion in Structural Biology
dc.relation.ispartofvolume14
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3101
dc.titleThe Sema Domain
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2004 Elsevier. Please refer to the journal's website for access to the definitive, published version.
gro.date.issued2004
gro.hasfulltextNo Full Text
gro.griffith.authorLove, Christopher A.


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