5A2F: Two Membrane Distal Igsf Domains Of Cd166

Citation:
Abstract
CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains. The membrane proximal domain of CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another cell surface receptor, CD166, which also engages in homophilic interactions. CD6 expression is mainly restricted to T cells, and the interaction between CD6 and CD166 regulates T-cell activation. We have solved the X-ray crystal structures of the three SRCR domains of CD6 and two N-terminal domains of CD166. This first structure of consecutive SRCR domains reveals a nonlinear organization. We characterized the binding sites on CD6 and CD166 and showed that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction. Native mass spectrometry analysis showed that there is competition between the heterophilic and homophilic interactions. These data give insight into how interactions of consecutive SRCR domains are perturbed by SNPs and potential therapeutic reagents.
PDB ID: 5A2FDownload
MMDB ID: 131155
PDB Deposition Date: 2015/5/18
Updated in MMDB: 2015/08
Experimental Method:
x-ray diffraction
Resolution: 1.86  Å
Source Organism:
Similar Structures:
Biological Unit for 5A2F: monomeric; determined by author and by software (PISA)
Molecular Components in 5A2F
Label Count Molecule
Protein (1 molecule)
1
Cd166 Antigen(Gene symbol: ALCAM)
Molecule annotation
Chemicals (18 molecules)
1
2
2
16
* Click molecule labels to explore molecular sequence information.

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