1OLZ

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

Summary for 1OLZ

• Entry DOI: 10.2210/pdb1olz/pdb
• Descriptor: SEMAPHORIN 4D (2 entities in total)
• Functional Keywords: developmental protein, cd100, semaphorin, beta-propeller, psi domain, ig-like domain, extracellular receptor, neurogenesis, glycoprotein developmental protein, structural proteomics in europe, spine, structural genomics
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 148631.09

Authors

Love, C.A.,Harlos, K.,Mavaddat, N.,Davis, S.J.,Stuart, D.I.,Jones, E.Y.,Esnouf, R.M. (deposition date: 2003-08-19, release date: 2003-09-11, Last modification date: 2024-11-13)

Primary citation

Love, C.A.,Harlos, K.,Mavaddat, N.,Davis, S.J.,Stuart, D.I.,Jones, E.Y.,Esnouf, R.M.
The Ligand-Binding Face of the Semaphorins Revealed by the High-Resolution Crystal Structure of Sema4D
Nat.Struct.Biol., 10:843-, 2003

PubMed 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.

PubMed: 12958590
DOI: 10.1038/NSB977

Experimental method

X-RAY DIFFRACTION (2 Å)