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

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...

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Publication status:
Published

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Publisher copy:
10.1038/nsb977

Authors


Mavaddat, N More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, RDM, Molecular Medicine
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
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Journal:
Nature structural biology
Volume:
10
Issue:
10
Pages:
843-848
Publication date:
2003-10-05
DOI:
ISSN:
1072-8368
URN:
uuid:8d2bff81-d19d-4754-9a17-b33465308fe5
Source identifiers:
24974
Local pid:
pubs:24974

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