2LGF: Solution Structure Of Ca2+/calmodulin Complexed With A Peptide Representing The Calmodulin-binding Domain Of L-selectin

The L-selectin glycoprotein receptor mediates the initial steps of leukocyte migration into secondary lymphoid organs and sites of inflammation. Following cell activation through the engagement of G-protein-coupled receptors or immunoreceptors, the extracellular domains of L-selectin are rapidly shed, a process negatively controlled via the binding of the ubiquitous eukaryotic calcium-binding protein calmodulin to the cytoplasmic tail of L-selectin. Here we present the solution structure of calcium-calmodulin bound to a peptide encompassing the cytoplasmic tail and part of the transmembrane domain of L-selectin. The structure and accompanying biophysical study highlight the importance of both calcium and the transmembrane segment of L-selectin in the interaction between these two proteins, suggesting that by binding this region, calmodulin regulates in an "inside-out" fashion the ectodomain shedding of the receptor. Our structure provides the first molecular insight into the emerging new role for calmodulin as a transmembrane signaling partner.
PDB ID: 2LGFDownload
MMDB ID: 138660
PDB Deposition Date: 2011/7/25
Updated in MMDB: 2016/06
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LGF: dimeric; determined by author
Molecular Components in 2LGF
Label Count Molecule
Proteins (2 molecules)
Molecule annotation
L-selectin(Gene symbol: SELL)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB