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New page: left|200px<br /> <applet load="1dr9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dr9, resolution 3.00Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1dr9.gif|left|200px]]<br />
<applet load="1dr9" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dr9, resolution 3.00&Aring;" />
'''CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)'''<br />


==Overview==
==CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)==
B7-1 (CD80) and B7-2 (CD86) are glycoproteins expressed on, antigen-presenting cells. The binding of these molecules to the T cell, homodimers CD28 and CTLA-4 (CD152) generates costimulatory and inhibitory, signals in T cells, respectively. The crystal structure of the, extracellular region of B7-1 (sB7-1), solved to 3 A resolution, consists, of a novel combination of two Ig-like domains, one characteristic of, adhesion molecules and the other previously seen only in antigen, receptors. In the crystal lattice, sB7-1 unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. Analytical ultracentrifugation, reveals that sB7-1 also dimerizes in solution. The structural data suggest, a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4, homodimers, along with the relatively high affinity of these interactions, favors the formation of very stable inhibitory signaling complexes.
<StructureSection load='1dr9' size='340' side='right'caption='[[1dr9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dr9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DR9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dr9 OCA], [https://pdbe.org/1dr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dr9 RCSB], [https://www.ebi.ac.uk/pdbsum/1dr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dr9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD80_HUMAN CD80_HUMAN] Involved in the costimulatory signal essential for T-lymphocyte activation. T-cell proliferation and cytokine production is induced by the binding of CD28 or CTLA-4 to this receptor.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dr/1dr9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dr9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
B7-1 (CD80) and B7-2 (CD86) are glycoproteins expressed on antigen-presenting cells. The binding of these molecules to the T cell homodimers CD28 and CTLA-4 (CD152) generates costimulatory and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-1), solved to 3 A resolution, consists of a novel combination of two Ig-like domains, one characteristic of adhesion molecules and the other previously seen only in antigen receptors. In the crystal lattice, sB7-1 unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. Analytical ultracentrifugation reveals that sB7-1 also dimerizes in solution. The structural data suggest a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4 homodimers, along with the relatively high affinity of these interactions, favors the formation of very stable inhibitory signaling complexes.


==About this Structure==
Structure and dimerization of a soluble form of B7-1.,Ikemizu S, Gilbert RJ, Fennelly JA, Collins AV, Harlos K, Jones EY, Stuart DI, Davis SJ Immunity. 2000 Jan;12(1):51-60. PMID:10661405<ref>PMID:10661405</ref>
1DR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DR9 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure and dimerization of a soluble form of B7-1., Ikemizu S, Gilbert RJ, Fennelly JA, Collins AV, Harlos K, Jones EY, Stuart DI, Davis SJ, Immunity. 2000 Jan;12(1):51-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10661405 10661405]
</div>
<div class="pdbe-citations 1dr9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Davis, S.J.]]
[[Category: Davis SJ]]
[[Category: Ikemizu, S.]]
[[Category: Ikemizu S]]
[[Category: Jones, E.Y.]]
[[Category: Jones EY]]
[[Category: Stuart, D.I.]]
[[Category: Stuart DI]]
[[Category: NAG]]
[[Category: ig superfamily]]
 
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