1cdc

<table><tr><td colspan='2'>[[1cdc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CDC 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=1cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cdc OCA], [https://pdbe.org/1cdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cdc RCSB], [https://www.ebi.ac.uk/pdbsum/1cdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cdc ProSAT]</span></td></tr>

[[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.

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== Publication Abstract from PubMed ==

When expressed as part of a glutathione S-transferase fusion protein the NH2-terminal domain of the lymphocyte cell adhesion molecule CD2 is shown to adopt two different folds. The immunoglobulin superfamily structure of the major (85%) monomeric component has previously been determined by both x-ray crystallography and NMR spectroscopy. We now describe the structure of a second, dimeric, form present in about 15% of recombinant CD2 molecules. After denaturation and refolding in the absence of the fusion partner, dimeric CD2 is converted to monomer, illustrating that the dimeric form represents a metastable folded state. The crystal structure of this dimeric form, refined to 2.0-A resolution, reveals two domains with overall similarity to the IgSF fold found in the monomer. However, in the dimer each domain is formed by the intercalation of two polypeptide chains. Hence each domain represents a distinct folding unit that can assemble in two different ways. In the dimer the two domains fold around a hydrophilic interface believed to mimic the cell adhesion interaction at the cell surface, and the formation of dimer can be regulated by mutating single residues at this interface. This unusual misfolded form of the protein, which appears to result from inter- rather than intramolecular interactions being favored by an intermediate structure formed during the folding process, illustrates that evolution of protein oligomers is possible from the sequence for a single protein domain.

One sequence, two folds: a metastable structure of CD2.,Murray AJ, Lewis SJ, Barclay AN, Brady RL Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7337-41. PMID:7638192<ref>PMID:7638192</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Barclay, A N]]

[[Category: Brady, R L]]

[[Category: Murray, A J]]

[[Category: Immune system protein]]

[[Category: Receptor]]