1o7v
From Proteopedia
|
HIGH RESOLUTION STRUCTURE OF SIGLEC-7
Overview
Sialic acid-binding immunoglobulin-like lectins (Siglecs) recognize, sialylated glycoconjugates and play a role in cell-cell recognition., Siglec-7 is expressed on natural killer cells and displays unique ligand, binding properties different from other members of the Siglec family. Here, we describe the high resolution structures of the N-terminal V-set Ig-like, domain of Siglec-7 in two crystal forms, at 1.75 and 1.9 A. The latter, crystal form reveals the full structure of this domain and allows us to, speculate on the differential ligand binding properties displayed by, members of the Siglec family. A fully ordered N-linked glycan is observed, tethered by tight interactions with symmetry-related protein molecules in, the crystal. Comparison of the structure with that of sialoadhesin and a, model of Siglec-9 shows that the unique preference of Siglec-7 for, alpha(2,8)-linked disialic acid is likely to reside in the C-C' loop, which is variable in the Siglec family. In the Siglec-7 structure, the, ligand-binding pocket is occupied by a loop of a symmetry-related, molecule, mimicking the interactions with sialic acid.
About this Structure
1O7V is a Single protein structure of sequence from Homo sapiens. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family., Alphey MS, Attrill H, Crocker PR, van Aalten DM, J Biol Chem. 2003 Jan 31;278(5):3372-7. Epub 2002 Nov 15. PMID:12438315
Page seeded by OCA on Mon Nov 5 16:45:58 2007
