dc.contributor.author | Love, CA | |
dc.contributor.author | Harlos, K | |
dc.contributor.author | Mavaddat, N | |
dc.contributor.author | Davis, SJ | |
dc.contributor.author | Stuart, DI | |
dc.contributor.author | Jones, EY | |
dc.contributor.author | Esnouf, RM | |
dc.date.accessioned | 2017-05-03T11:37:23Z | |
dc.date.available | 2017-05-03T11:37:23Z | |
dc.date.issued | 2003 | |
dc.date.modified | 2009-09-03T07:14:39Z | |
dc.identifier.issn | 1072-8368 | |
dc.identifier.doi | 10.1038/nsb977 | |
dc.identifier.uri | http://hdl.handle.net/10072/16925 | |
dc.description.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 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.peerreviewed | Yes | |
dc.description.publicationstatus | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Nature Publishing Group | |
dc.publisher.place | United States | |
dc.publisher.uri | http://www.nature.com/nsmb/index.html | |
dc.relation.ispartofpagefrom | 843 | |
dc.relation.ispartofpageto | 848 | |
dc.relation.ispartofissue | 10 | |
dc.relation.ispartofjournal | Nature Structural Biology | |
dc.relation.ispartofvolume | 10 | |
dc.subject.fieldofresearch | Chemical sciences | |
dc.subject.fieldofresearch | Biological sciences | |
dc.subject.fieldofresearch | Biomedical and clinical sciences | |
dc.subject.fieldofresearchcode | 34 | |
dc.subject.fieldofresearchcode | 31 | |
dc.subject.fieldofresearchcode | 32 | |
dc.title | The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - 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.issued | 2003 | |
gro.hasfulltext | No Full Text | |
gro.griffith.author | Love, Christopher A. | |