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[[Image:1a6p.gif|left|200px]]
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{{STRUCTURE_1a6p|  PDB=1a6p  |  SCENE=  }}
'''ENGINEERING OF A MISFOLDED FORM OF CD2'''


==ENGINEERING OF A MISFOLDED FORM OF CD2==
<StructureSection load='1a6p' size='340' side='right'caption='[[1a6p]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1a6p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A6P 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]] 2.08&#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=1a6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6p OCA], [https://pdbe.org/1a6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6p RCSB], [https://www.ebi.ac.uk/pdbsum/1a6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD2_RAT CD2_RAT] 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 ==
[[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/a6/1a6p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1a6p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The amino-terminal domain of CD2 has the remarkable ability to fold in two ways: either as a monomer or as an intertwined, metastable dimer. Here we show that it is possible to differentially stabilize either fold by engineering the CD2 sequence, mimicking random mutagenesis events that could occur during molecular evolution. Crystal structures of a hinge-deletion mutant, which is stable as an intertwined dimer, reveal domain rotations that enable the protein to further assemble to a tetramer. These results demonstrate that a variety of folds can be adopted by a single polypeptide sequence, and provide guidance for the design of proteins capable of further assembly.


==Overview==
Engineering an intertwined form of CD2 for stability and assembly.,Murray AJ, Head JG, Barker JJ, Brady RL Nat Struct Biol. 1998 Sep;5(9):778-82. PMID:9731771<ref>PMID:9731771</ref>
The amino-terminal domain of CD2 has the remarkable ability to fold in two ways: either as a monomer or as an intertwined, metastable dimer. Here we show that it is possible to differentially stabilize either fold by engineering the CD2 sequence, mimicking random mutagenesis events that could occur during molecular evolution. Crystal structures of a hinge-deletion mutant, which is stable as an intertwined dimer, reveal domain rotations that enable the protein to further assemble to a tetramer. These results demonstrate that a variety of folds can be adopted by a single polypeptide sequence, and provide guidance for the design of proteins capable of further assembly.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1A6P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6P OCA].
</div>
<div class="pdbe-citations 1a6p" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Engineering an intertwined form of CD2 for stability and assembly., Murray AJ, Head JG, Barker JJ, Brady RL, Nat Struct Biol. 1998 Sep;5(9):778-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9731771 9731771]
*[[CD2|CD2]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Barker JJ]]
[[Category: Barker, J J.]]
[[Category: Brady RL]]
[[Category: Brady, R L.]]
[[Category: Head JG]]
[[Category: Head, J G.]]
[[Category: Murray AJ]]
[[Category: Murray, A J.]]
[[Category: Cell adhesion]]
[[Category: Domain swapping]]
[[Category: Hinge loop]]
[[Category: Oligomer evolution]]
[[Category: T lymphocyte adhesion glycoprotein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:53:44 2008''

Latest revision as of 10:48, 2 August 2023

ENGINEERING OF A MISFOLDED FORM OF CD2

1a6p, resolution 2.08Å

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