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VEK-30 protein domain

In molecular biology, the protein domain VEK-30, is a 30-amino acid long, internal peptide present within bacterial organisms that acts as an epitope or antigenic determinant. It increases the pathogenicity of the cell. More specifically, it is found in streptococcal M-like plasminogen (Pg)-binding protein (PAM) from gram-positive group-A streptococci (GAS). VEK-30 represents an epitope within PAM that shows high affinity for the lysine binding site (LBS) of the kringle-2 (K2) domain of human (h)Pg.

VEK-30
the x-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound a to a peptide from the group a streptococcal surface protein pam
Identifiers
SymbolVEK-30
PfamPF12107
InterProIPR021965
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Plasminogen edit

Plasminogen (Pg) is an important mediator of angiostatin production in the fibrinolytic pathway. Plasminogen is made up of five subunit kringle molecules (Pg-K1 to Pg-K5), of which the first three make the protein angiostatin. VEK-30 is a protein domain of the group A streptococcal protein PAM. It binds to Pg-K2 domain of angiostatin and activates the molecule to mediate its anti-angiogenic effects. VEK-30 binds to angiostatin via a C-terminal lysine with argininyl and glutamyl side chain residues known as a 'through space isostere'.[1]

Function edit

Since VEK-30 binds to Pg-K2 domain of angiostatin, its function is crucial to blood clotting, and in lower organisms increase their pathogenicity.

Structure edit

In solution, it has been found that VEK-30, exhibited the canonical fold of a kringle domain, including a lack of regular secondary structure.[2]

References edit

  1. ^ Cnudde SE, Prorok M, Castellino FJ, Geiger JH (September 2006). "X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcal surface protein PAM". Biochemistry. 45 (37): 11052–60. doi:10.1021/bi060914j. PMID 16964966.
  2. ^ Wang M, Zajicek J, Geiger JH, Prorok M, Castellino FJ (2010). "Solution structure of the complex of VEK-30 and plasminogen kringle 2". J Struct Biol. 169 (3): 349–59. doi:10.1016/j.jsb.2009.09.011. PMC 2826548. PMID 19800007.
This article incorporates text from the public domain Pfam and InterPro: IPR021965

protein, domain, molecular, biology, protein, domain, amino, acid, long, internal, peptide, present, within, bacterial, organisms, that, acts, epitope, antigenic, determinant, increases, pathogenicity, cell, more, specifically, found, streptococcal, like, plas. In molecular biology the protein domain VEK 30 is a 30 amino acid long internal peptide present within bacterial organisms that acts as an epitope or antigenic determinant It increases the pathogenicity of the cell More specifically it is found in streptococcal M like plasminogen Pg binding protein PAM from gram positive group A streptococci GAS VEK 30 represents an epitope within PAM that shows high affinity for the lysine binding site LBS of the kringle 2 K2 domain of human h Pg VEK 30the x ray crystallographic structure of the angiogenesis inhibitor angiostatin bound a to a peptide from the group a streptococcal surface protein pamIdentifiersSymbolVEK 30PfamPF12107InterProIPR021965Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Plasminogen 2 Function 3 Structure 4 ReferencesPlasminogen editPlasminogen Pg is an important mediator of angiostatin production in the fibrinolytic pathway Plasminogen is made up of five subunit kringle molecules Pg K1 to Pg K5 of which the first three make the protein angiostatin VEK 30 is a protein domain of the group A streptococcal protein PAM It binds to Pg K2 domain of angiostatin and activates the molecule to mediate its anti angiogenic effects VEK 30 binds to angiostatin via a C terminal lysine with argininyl and glutamyl side chain residues known as a through space isostere 1 Function editSince VEK 30 binds to Pg K2 domain of angiostatin its function is crucial to blood clotting and in lower organisms increase their pathogenicity Structure editIn solution it has been found that VEK 30 exhibited the canonical fold of a kringle domain including a lack of regular secondary structure 2 References edit Cnudde SE Prorok M Castellino FJ Geiger JH September 2006 X ray crystallographic structure of the angiogenesis inhibitor angiostatin bound to a peptide from the group A streptococcal surface protein PAM Biochemistry 45 37 11052 60 doi 10 1021 bi060914j PMID 16964966 Wang M Zajicek J Geiger JH Prorok M Castellino FJ 2010 Solution structure of the complex of VEK 30 and plasminogen kringle 2 J Struct Biol 169 3 349 59 doi 10 1016 j jsb 2009 09 011 PMC 2826548 PMID 19800007 This article incorporates text from the public domain Pfam and InterPro IPR021965 Retrieved from https en wikipedia org w index php title VEK 30 protein domain amp oldid 1095346966, wikipedia, wiki, book, books, library,

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