1lmt
From Proteopedia
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STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME
Overview
To examine the effect of a conformational constraint introduced into the, Arg-Gly-Asp (RGD) sequence on cell adhesion activity, we constructed a, mutant protein by inserting an RGD-containing sequence flanked by two Cys, residues between Val74 and Asn75 of human lysozyme. The CRGDSC-inserted, lysozyme was expressed in yeast, purified, and designated as Cys-RGD4., Using baby hamster kidney cells, Cys-RGD4 was shown to possess even higher, cell adhesion activity than that of the RGDS-inserted lysozyme, RGD4. The, Cys-RGD4 protein was co-crystallized with a lysozyme inhibitor, tri-N-acetylchitotriose, and the three-dimensional structure was, determined at 1.6-A resolution by x-ray crystallography. In contrast to, RGD4, the inserted RGD-containing region of Cys-RGD4 was well defined. The, structural analysis revealed that the two inserted Cys residues form a new, disulfide bond in Cys-RGD4, as expected, and that the RGD region assumes a, type II' beta-turn conformation of Gly-Asp with a hydrogen bond between, the C = O of Arg and the H-N of Ser. In addition, it was confirmed that, two more hydrogen bonds are present in the RGD region of the Cys-RGD4, lysozyme. These results suggest that the conformation of the, RGD-containing region is rigid and stable in the Cys-RGD4 molecule and, that the type II' beta-turn structure of RGD is essential for binding to, integrins with high affinity.
About this Structure
1LMT is a Single protein structure of sequence from Homo sapiens with CL as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme., Yamada T, Song H, Inaka K, Shimada Y, Kikuchi M, Matsushima M, J Biol Chem. 1995 Mar 17;270(11):5687-90. PMID:7890692
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