2LGF

Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin

Summary for 2LGF

• Entry DOI: 10.2210/pdb2lgf/pdb
• NMR Information: BMRB: 17807
• Descriptor: Calmodulin, L-selectin, CALCIUM ION (3 entities in total)
• Functional Keywords: metal binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton, spindle : P62158; Membrane; Single-pass type I membrane protein: P14151
• Total number of polymer chains: 2
• Total formula weight: 18644.93

Authors

Gifford, J.L.,Ishida, H.,Vogel, H.J. (deposition date: 2011-07-25, release date: 2012-06-13, Last modification date: 2024-05-15)

Primary citation

Gifford, J.L.,Ishida, H.,Vogel, H.J.
Structural Insights into Calmodulin-regulated L-selectin Ectodomain Shedding.
J.Biol.Chem., 287:26513-26527, 2012

PubMed Abstract: 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.

PubMed: 22711531
DOI: 10.1074/jbc.M112.373373

Experimental method

SOLUTION NMR