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| {{STRUCTURE_1ncn| PDB=1ncn | SCENE= }} | | {{STRUCTURE_1ncn| PDB=1ncn | SCENE= }} |
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| '''the receptor-binding domain of human B7-2'''
| | ===the receptor-binding domain of human B7-2=== |
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| ==Overview==
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| B7-1 and B7-2 are homologous costimulatory ligands expressed on the surfaces of antigen-presenting cells. Their interactions with CD28/CTLA-4 receptors expressed on T cell surfaces are crucial for the proper regulation of T cell activity. B7-1 and B7-2 display distinct roles in immune regulation, although they are usually considered to have redundant functions. Here, we report the crystal structure of the receptor-binding (Ig V-type) domain of human B7-2 at 2.7-A resolution. Structures of unliganded and liganded B7-1 and B7-2 suggest a physical-chemical basis for the observed functional similarities and differences between these two costimulatory ligands. Of particular note, whereas the majority of the residues mediating B7-1 dimerization are hydrophobic, the B7-2 dimer observed in the B7-2/CTLA-4 complex displays a very hydrophilic dimer interface. These differences provide a mechanism for preventing the formation of B7-1/B7-2 heterodimers. The divergence at the putative dimer interface is also consistent with the lower tendency of B7-2 to dimerize, as shown by the monomeric state of unliganded B7-2 both in solution and crystalline form, and may result in detailed differences in signaling mechanisms associated with B7-1 and B7-2.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12606712}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12606712 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12606712}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta strand]] | | [[Category: Beta strand]] |
| [[Category: Ig v]] | | [[Category: Ig v]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:22:28 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:01:12 2008'' |
