![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
![[thumbnail of 8130oa.pdf]](https://mdc-test.eprints-hosting.org/style/images/fileicons/application_pdf.png) |
PDF
- Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
901kB |
| Item Type: | Article |
|---|---|
| Title: | X-ray structure of engineered human Aortic Preferentially Expressed Protein-1 (APEG-1) |
| Creators Name: | Manjasetty, B.A., Niesen, F.H., Scheich, C., Roske, Y., Goetz, F., Behlke, J., Sievert, V., Heinemann, U. and Buessow, K. |
| Abstract: | BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a novel specific smooth muscle differentiation marker thought to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). RESULTS: Good quality crystals that were suitable for X-ray crystallographic studies were obtained following the truncation of the 14 N-terminal amino acids of APEG-1, a region predicted to be disordered. The truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition motif. The RGD motif is crucial for the interaction of extracellular proteins and plays a role in cell adhesion. The X-ray structure of DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96 A). This is the best resolution for an immunoglobulin domain structure so far. The structure adopts a Greek-key beta-sandwich fold and belongs to the I (intermediate) set of the immunoglobulin superfamily. The residues lying between the beta-sheets form a hydrophobic core. The RGD motif folds into a 310 helix that is involved in the formation of a homodimer in the crystal which is mainly stabilized by salt bridges. Analytical ultracentrifugation studies revealed a moderate dissociation constant of 20 microM at physiological ionic strength, suggesting that APEG-1 dimerisation is only transient in the cell. The binding constant is strongly dependent on ionic strength. CONCLUSION: Our data suggests that the RGD motif might play a role not only in the adhesion of extracellular proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of APEG-1 involving this motif is physiologically relevant. |
| Keywords: | Amino Acid Motifs, Amino Acid Sequence, Arteries, Biophysics, Cell Adhesion, Molecular Cloning, X-Ray Crystallography, Protein Databases, Dimerization, Escherichia ColiImmunoglobulins, Kinetics, Lysine, Molecular Models, Molecular Sequence Data, Muscle Proteins, Smooth Muscle Myocytes |
| Source: | BMC Structural Biology |
| ISSN: | 1472-6807 |
| Publisher: | BioMed Central |
| Volume: | 5 |
| Number: | 14 |
| Page Range: | 21 |
| Date: | 14 December 2005 |
| Official Publication: | https://doi.org/10.1186/1472-6807-5-21 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
