1qa9: Difference between revisions

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<StructureSection load='1qa9' size='340' side='right'caption='[[1qa9]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='1qa9' size='340' side='right'caption='[[1qa9]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qa9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QA9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qa9]] is a 4 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=1QA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QA9 FirstGlance]. <br>
</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=1qa9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qa9 OCA], [https://pdbe.org/1qa9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qa9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qa9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qa9 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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=1qa9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qa9 OCA], [https://pdbe.org/1qa9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qa9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qa9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qa9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD2_HUMAN CD2_HUMAN] CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1qa9 ConSurf].
</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=1qa9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interaction between CD2 and its counterreceptor, CD58 (LFA-3), on opposing cells optimizes immune recognition, facilitating contacts between helper T lymphocytes and antigen-presenting cells as well as between cytolytic effectors and target cells. Here, we report the crystal structure of the heterophilic adhesion complex between the amino-terminal domains of human CD2 and CD58. A strikingly asymmetric, orthogonal, face-to-face interaction involving the major beta sheets of the respective immunoglobulin-like domains with poor shape complementarity is revealed. In the virtual absence of hydrophobic forces, interdigitating charged amino acid side chains form hydrogen bonds and salt links at the interface (approximately 1200 A2), imparting a high degree of specificity albeit with low affinity (K(D) of approximately microM). These features explain CD2-CD58 dynamic binding, offering insights into interactions of related immunoglobulin superfamily receptors.
Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors.,Wang JH, Smolyar A, Tan K, Liu JH, Kim M, Sun ZY, Wagner G, Reinherz EL Cell. 1999 Jun 11;97(6):791-803. PMID:10380930<ref>PMID:10380930</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qa9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[CD2|CD2]]
*[[CD2|CD2]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kim, M]]
[[Category: Kim M]]
[[Category: Liu, J H]]
[[Category: Liu J-H]]
[[Category: Reinherz, E L]]
[[Category: Reinherz EL]]
[[Category: Smolyar, A]]
[[Category: Smolyar A]]
[[Category: Sun, Z J]]
[[Category: Sun ZJ]]
[[Category: Tan, K]]
[[Category: Tan K]]
[[Category: Wagner, G]]
[[Category: Wagner G]]
[[Category: Wang, J H]]
[[Category: Wang J-H]]
[[Category: Cd2]]
[[Category: Cd58]]
[[Category: Cell adhesion]]
[[Category: Ig-like domain]]
[[Category: Immune system]]

Latest revision as of 08:14, 14 February 2024

Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors

1qa9, resolution 3.20Å

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