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1ncn

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[[Image:1ncn.gif|left|200px]]
[[Image:1ncn.gif|left|200px]]
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{{Structure
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|GENE= B7-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1ncn| PDB=1ncn | SCENE= }}
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|RELATEDENTRY=[[1i85|1I85]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ncn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ncn OCA], [http://www.ebi.ac.uk/pdbsum/1ncn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ncn RCSB]</span>
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'''the receptor-binding domain of human B7-2'''
'''the receptor-binding domain of human B7-2'''
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[[Category: Schwartz, J D.]]
[[Category: Schwartz, J D.]]
[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
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[[Category: beta strand]]
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[[Category: Beta strand]]
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[[Category: ig v]]
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[[Category: Ig v]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:22:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:31 2008''
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Revision as of 23:22, 2 May 2008

Template:STRUCTURE 1ncn

the receptor-binding domain of human B7-2


Overview

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.

About this Structure

1NCN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the receptor-binding domain of human B7-2: insights into organization and signaling., Zhang X, Schwartz JC, Almo SC, Nathenson SG, Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2586-91. Epub 2003 Feb 26. PMID:12606712 Page seeded by OCA on Sat May 3 02:22:28 2008

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