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Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen.

Chang Y, Mochalkin I, McCance SG, Cheng B, Tulinsky A, Castellino FJ
Biochemistry 37 3258-71 (1998)
Cited: 45 times
EuropePMC logo PMID: 9521645

Abstract

The X-ray crystal structure of the recombinant (r) kringle 5 domain of human plasminogen (K5HPg) has been solved by molecular replacement methods using K1HPg as a model and refined at 1.7 A resolution to an R factor of 16.6%. The asymmetric unit of K5HPg is composed of two molecules related by a noncrystallographic 2-fold rotation axis approximately parallel to the z-direction. The lysine binding site (LBS) is defined by the regions His33-Thr37, Pro54-Val58, Pro61-Tyr64, and Leu71-Tyr74 and is occupied in the apo-form by water molecules. A unique feature of the LBS of apo-K5HPg is the substitution by Leu71 for the basic amino acid, arginine, that in other kringle polypeptides forms the donor cationic center for the carboxylate group of omega-amino acid ligands. While wild-type (wt) r-K5HPg interacted weakly with these types of ligands, replacement by site-directed mutagenesis of Leu71 by arginine led to substantially increased affinity of the ligands for the LBS of K5HPg. As a result, binding of omega-amino acids to this mutant kringle (r-K5HPg[L71R]) was restored to levels displayed by the companion much stronger affinity HPg kringles, K1HPg and K4HPg. Correspondingly, alkylamine binding to r-K5HPg[L71R] was considerably attenuated from that shown by wtr-K5HPg. Thus, employing a rational design strategy based on the crystal structure of K5HPg, successful remodeling of the LBS has been accomplished, and has resulted in the conversion of a weak ligand binding kringle to one that possesses an affinity for omega-amino acids that is similar to K1HPg and K4HPg.

Articles - 5hpg mentioned but not cited (6)

  1. Plasminogen alleles influence susceptibility to invasive aspergillosis. Zaas AK, Liao G, Chien JW, Weinberg C, Shore D, Giles SS, Marr KA, Usuka J, Burch LH, Perera L, Perfect JR, Peltz G, Schwartz DA. PLoS Genet 4 e1000101 (2008)
  2. Plasminogen substrate recognition by the streptokinase-plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase beta-domain and kringle 5 of the substrate. Tharp AC, Laha M, Panizzi P, Thompson MW, Fuentes-Prior P, Bock PE. J Biol Chem 284 19511-19521 (2009)
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  4. Identification and analyses of inhibitors targeting apolipoprotein(a) kringle domains KIV-7, KIV-10, and KV provide insight into kringle domain function. Sandmark J, Tigerström A, Akerud T, Althage M, Antonsson T, Blaho S, Bodin C, Boström J, Chen Y, Dahlén A, Eriksson PO, Evertsson E, Fex T, Fjellström O, Gustafsson D, Herslöf M, Hicks R, Jarkvist E, Johansson C, Kalies I, Karlsson Svalstedt B, Kartberg F, Legnehed A, Martinsson S, Moberg A, Ridderström M, Rosengren B, Sabirsh A, Thelin A, Vinblad J, Wellner AU, Xu B, Östlund-Lindqvist AM, Knecht W. J Biol Chem 295 5136-5151 (2020)
  5. A computational peptide model induces cancer cells' apoptosis by docking Kringle 5 to GRP78. Khater I, Nassar A. BMC Mol Cell Biol 24 25 (2023)
  6. Voltage-Dependent Anion Channel-1, a Possible Ligand of Plasminogen Kringle 5. Liang YK, Bian LJ. PLoS One 11 e0164834 (2016)


Reviews citing this publication (7)

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  7. Understanding the fluorescence changes of human plasminogen when it binds the ligand, 6-aminohexanoate: a synthesis. Kornblatt JA. Biochim Biophys Acta 1481 1-10 (2000)

Articles citing this publication (32)

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  11. The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains. Gehrmann M, Briknarová K, Bányai L, Patthy L, Llinás M. Biol Chem 383 137-148 (2002)
  12. Skizzle is a novel plasminogen- and plasmin-binding protein from Streptococcus agalactiae that targets proteins of human fibrinolysis to promote plasmin generation. Wiles KG, Panizzi P, Kroh HK, Bock PE. J Biol Chem 285 21153-21164 (2010)
  13. High-resolution crystal structure of apolipoprotein(a) kringle IV type 7: insights into ligand binding. Ye Q, Rahman MN, Koschinsky ML, Jia Z. Protein Sci 10 1124-1129 (2001)
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  19. Dimerization is not a determining factor for functional high affinity human plasminogen binding by the group A streptococcal virulence factor PAM and is mediated by specific residues within the PAM a1a2 domain. Bhattacharya S, Liang Z, Quek AJ, Ploplis VA, Law R, Castellino FJ. J Biol Chem 289 21684-21693 (2014)
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  31. Prostate Cancer-Specific of DD3-driven Oncolytic Virus-harboring mK5 Gene. Hao J, Xie W, Li H, Li R. Open Med (Wars) 14 1-9 (2019)
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