Limits...
Amino Acid Sequences Mediating Vascular Cell Adhesion Molecule 1 Binding to Integrin Alpha 4: Homologous DSP Sequence Found for JC Polyoma VP1 Coat Protein.

Meyer MA - Neurol Int (2013)

Bottom Line: The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1.Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3).Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Tennova Health Care , Knoxville, TN, USA.

ABSTRACT
The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1. Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3). For the JC polyoma virus, a DSP sequence was found at residues 70, 71 and 72 with homology also noted for the mouse polyoma virus and SV40 virus. Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.

No MeSH data available.


Related in: MedlinePlus

The VP1 protein as a ball and stick representation colored according to charge, with yellow indicating the DSP sequence homologous to the IDSP sequence mediating VCAM-1 binding to the alpha 4 integrin molecule.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC3794449&req=5

fig003: The VP1 protein as a ball and stick representation colored according to charge, with yellow indicating the DSP sequence homologous to the IDSP sequence mediating VCAM-1 binding to the alpha 4 integrin molecule.

Mentions: Although the full IDSP sequence was not found, a DSP sequence was found for the JC polyoma virus VP1 coat protein (accession number P03089) as well as Mouse polyomavirus (strain p16 small-plaque; accession-number 1SIE_A), as well as Chain 1, Simian Virus 40 (accession number 1SVA_1), but not for Kilham polyomavirus (accession number P24595), Budgerigar fledgling polyomavirus (BFPyV; accession number P13891), Hamster polyomavirus (HaPyV; accession number P03092), African green monkey polyomavirus (accession number P04010), or Bovine polyomavirus (accession number P24848). Alligned short segments of VP1 which display the homologous DSP sequence are shown in red in Figure 1 with residues 70,71, and 72 for the JC polyoma virus being aspartic acid (D), serine (S), and proline (P) respectively. The three dimensional external view of a single pentamer capsid (Figure 2) reveals accessible DSP residues for interaction and potential ligand binding. A detailed interactive review of a ball and stick type model (Figure 3) one of the five individual molecules that form a pentamer suggests a peripheral location to the DSP loop in relation to the bulk of the VP1 molecule, with the suggestion that a pocket is formed by this eccentric peripheral loop that could allow insertion of a small ligand molecule into this site.


Amino Acid Sequences Mediating Vascular Cell Adhesion Molecule 1 Binding to Integrin Alpha 4: Homologous DSP Sequence Found for JC Polyoma VP1 Coat Protein.

Meyer MA - Neurol Int (2013)

The VP1 protein as a ball and stick representation colored according to charge, with yellow indicating the DSP sequence homologous to the IDSP sequence mediating VCAM-1 binding to the alpha 4 integrin molecule.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3794449&req=5

fig003: The VP1 protein as a ball and stick representation colored according to charge, with yellow indicating the DSP sequence homologous to the IDSP sequence mediating VCAM-1 binding to the alpha 4 integrin molecule.
Mentions: Although the full IDSP sequence was not found, a DSP sequence was found for the JC polyoma virus VP1 coat protein (accession number P03089) as well as Mouse polyomavirus (strain p16 small-plaque; accession-number 1SIE_A), as well as Chain 1, Simian Virus 40 (accession number 1SVA_1), but not for Kilham polyomavirus (accession number P24595), Budgerigar fledgling polyomavirus (BFPyV; accession number P13891), Hamster polyomavirus (HaPyV; accession number P03092), African green monkey polyomavirus (accession number P04010), or Bovine polyomavirus (accession number P24848). Alligned short segments of VP1 which display the homologous DSP sequence are shown in red in Figure 1 with residues 70,71, and 72 for the JC polyoma virus being aspartic acid (D), serine (S), and proline (P) respectively. The three dimensional external view of a single pentamer capsid (Figure 2) reveals accessible DSP residues for interaction and potential ligand binding. A detailed interactive review of a ball and stick type model (Figure 3) one of the five individual molecules that form a pentamer suggests a peripheral location to the DSP loop in relation to the bulk of the VP1 molecule, with the suggestion that a pocket is formed by this eccentric peripheral loop that could allow insertion of a small ligand molecule into this site.

Bottom Line: The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1.Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3).Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Tennova Health Care , Knoxville, TN, USA.

ABSTRACT
The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1. Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3). For the JC polyoma virus, a DSP sequence was found at residues 70, 71 and 72 with homology also noted for the mouse polyoma virus and SV40 virus. Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.

No MeSH data available.


Related in: MedlinePlus