Journal article
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
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Authors
Bibliographic Details
- Journal:
- Nature structural biology
- Volume:
- 10
- Issue:
- 10
- Pages:
- 843-848
- Publication date:
- 2003-10-01
- DOI:
- ISSN:
-
1072-8368
- Source identifiers:
-
24974
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:24974
- UUID:
-
uuid:8d2bff81-d19d-4754-9a17-b33465308fe5
- Local pid:
- pubs:24974
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2003
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