PMID: 16169851

 

    Legend: Gene, Sites

Title : Attenuating lymphocyte activity: the crystal structure of the BTLA- HVEM complex

Abstract :

1. Five CD28-like proteins exert positive or negative effects on immune cells
2. Only four of these five receptors interact with members of the B7 family
3. The exception is BTLA ( B and T lymphocyte attenuator ), which instead interacts with the tumor necrosis factor receptor superfamily member HVEM ( herpes virus entry mediator )
4. To better understand this interaction, we determined the 2.8-A crystal structure of the BTLA- HVEM complex
5. This structure shows that BTLA binds the N-terminal cysteine-rich domain of HVEM and employs a unique binding surface compared with other CD28-like receptors
6. Moreover, the structure shows that BTLA recognizes the same surface on HVEM as gD (herpes virus glycoprotein D ) and utilizes a similar binding motif
7. Light scattering analysis demonstrates that the extracellular domain of BTLA is monomeric and that BTLA and HVEM form a 1:1 complex
8. Alanine-scanning mutagenesis of HVEM was used to further define critical binding residues
9. Finally, BTLA adopts an immunoglobulin I-set fold
10. Despite structural similarities to other CD28-like members, BTLA represents a unique co-receptor

Output (sent_index, trigger, protein, sugar, site):

• 6. glycoprotein, , glycoprotein D, -, -

Output(Part-Of) (sent_index, protein, site):

• 5. HVEM, domain
• 7. BTLA, domain

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
structure of the BTLA	151888	0,4
HVEM	8764	0,3,4,5,6,7,8
B and T lymphocyte attenuator	151888	3
BTLA	151888	3,5,6,7,10
Finally, BTLA	151888	9
herpes virus entry mediator	8764	3
glycoprotein D	2532	6