1OLZ
The ligand-binding face of the semaphorins revealed by the high resolution crystal structure of SEMA4D
1OLZ の概要
| エントリーDOI | 10.2210/pdb1olz/pdb |
| 分子名称 | SEMAPHORIN 4D (2 entities in total) |
| 機能のキーワード | developmental protein, cd100, semaphorin, beta-propeller, psi domain, ig-like domain, extracellular receptor, neurogenesis, glycoprotein developmental protein, structural proteomics in europe, spine, structural genomics |
| 由来する生物種 | Homo sapiens (Human) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 148631.09 |
| 構造登録者 | Love, C.A.,Harlos, K.,Mavaddat, N.,Davis, S.J.,Stuart, D.I.,Jones, E.Y.,Esnouf, R.M. (登録日: 2003-08-19, 公開日: 2003-09-11, 最終更新日: 2024-11-13) |
| 主引用文献 | 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 Cited by 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: 12958590DOI: 10.1038/NSB977 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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