Crystal Structure of P-selectin Lectin/EGF domains
During inflammation, leukocytes tether and roll on the walls of vessels where they are to become active. E-, L- and P-selectin proteins are the primary units responsible for the tethering and rolling of these leukocytes. The following is a series of images of the crystalline structure of the P-selectin complex.
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One of the domains in P-selectin is the B chain:
Another domain similar to the B chain of P-selectin is the Colipase domain:
There are various ligands associated with the P-selectin complex. These are 4 calcium ions (shown as single spherical units) and 2 MPD heteroatoms (2-methyl-2,4-Pentanediol).
P-selectin is not a membrane protein. It can be found circulating in the blood. Because of this, the protein hydrophilically interacts with water molecules.
The active site of P-selectin is of Ser, His and Asp residues:
*Note: when zooming in or out on an image, click the button two times to achieve the desired magnification.
References:
*W. D. Hanley, K Konstantopoulos and D. Wirtz, "Receptor-Ligand Binding: 'Catch' Bonds Finally Caught"
Current Biology, Volume 13, R611-R613: August 5, 2003.
*W. S. Somers, J. Tand, G. D. Shaw, R. T. Camphausen, "Insights into the molecular basis of Leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to slex and PSGL-1"
Cell, Volume 103, page 467: 2000.
*N. Silva and D. Marcey, "An Introduction to Chime Scripting", David Marcey 2001
This project was completed by Chad Powers and Annalisa Jordan (Fall 2003)