1a64: Difference between revisions
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<StructureSection load='1a64' size='340' side='right'caption='[[1a64]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1a64' size='340' side='right'caption='[[1a64]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a64]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1a64]] 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=1A64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A64 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=1a64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a64 OCA], [https://pdbe.org/1a64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a64 RCSB], [https://www.ebi.ac.uk/pdbsum/1a64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a64 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]] 2Å</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=1a64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a64 OCA], [https://pdbe.org/1a64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a64 RCSB], [https://www.ebi.ac.uk/pdbsum/1a64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a64 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Barker JJ]] | ||
[[Category: | [[Category: Brady RL]] | ||
[[Category: | [[Category: Head JG]] | ||
[[Category: | [[Category: Murray AJ]] | ||
Latest revision as of 13:47, 2 August 2023
ENGINEERING A MISFOLDED FORM OF RAT CD2ENGINEERING A MISFOLDED FORM OF RAT CD2
Structural highlights
FunctionCD2_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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