Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases - PubMed (original) (raw)
Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases
L Patthy et al. FEBS Lett. 1984.
Free article
Abstract
Prothrombin, plasminogen, urokinase- and tissue-type plasminogen activators contain homologous structures known as kringles . The kringles correspond to autonomous structural and folding domains which mediate the binding of these multidomain proteins to other proteins. During evolution the different kringles retained the same gross architecture, the kringle -fold, yet diverged to bind different proteins. We show that the amino acid sequences of the type II structures of the gelatin-binding region of fibronectin are homologous with those of the protease- kringles . Prediction of secondary structures revealed a remarkable agreement in the positions of predicted beta-sheets, suggesting that the folding of kringles and type II structures may also be similar. As a corollary of this finding, the disulphide-bridge pattern of type II structures is shown to be homologous to that in kringles . It is noteworthy that protease- kringles and fibronectin type II structures have similar functions inasmuch as they mediate the binding of multidomain proteins to other proteins. It is proposed that the kringles of proteases and type II structures of fibronectin evolved from a common ancestral protein binding module.
Similar articles
- Common evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator.
Bányai L, Váradi A, Patthy L. Bányai L, et al. FEBS Lett. 1983 Oct 31;163(1):37-41. doi: 10.1016/0014-5793(83)81157-0. FEBS Lett. 1983. PMID: 6685059 - Apolipoprotein(a): structure-function relationship at the lysine-binding site and plasminogen activator cleavage site.
Anglés-Cano E, Rojas G. Anglés-Cano E, et al. Biol Chem. 2002 Jan;383(1):93-9. doi: 10.1515/BC.2002.009. Biol Chem. 2002. PMID: 11928826 Review. - Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules.
Patthy L. Patthy L. Cell. 1985 Jul;41(3):657-63. doi: 10.1016/s0092-8674(85)80046-5. Cell. 1985. PMID: 3891096 Review. No abstract available.
Cited by
- A central CRMP complex essential for invasion in Toxoplasma gondii.
Singer M, Simon K, Forné I, Meissner M. Singer M, et al. PLoS Biol. 2023 Jan 5;21(1):e3001937. doi: 10.1371/journal.pbio.3001937. eCollection 2023 Jan. PLoS Biol. 2023. PMID: 36602948 Free PMC article. - An apical membrane complex for triggering rhoptry exocytosis and invasion in Toxoplasma.
Sparvoli D, Delabre J, Penarete-Vargas DM, Kumar Mageswaran S, Tsypin LM, Heckendorn J, Theveny L, Maynadier M, Mendonça Cova M, Berry-Sterkers L, Guérin A, Dubremetz JF, Urbach S, Striepen B, Turkewitz AP, Chang YW, Lebrun M. Sparvoli D, et al. EMBO J. 2022 Nov 17;41(22):e111158. doi: 10.15252/embj.2022111158. Epub 2022 Oct 17. EMBO J. 2022. PMID: 36245278 Free PMC article. - Different N-Glycosylation Sites Reduce the Activity of Recombinant DSPAα2.
Peng H, Wang M, Wang N, Yang C, Guo W, Li G, Huang S, Wei D, Liu D. Peng H, et al. Curr Issues Mol Biol. 2022 Aug 31;44(9):3930-3947. doi: 10.3390/cimb44090270. Curr Issues Mol Biol. 2022. PMID: 36135182 Free PMC article. - Genetic Analysis of a Pedigree With Antithrombin and Prothrombin Compound Mutations and Antithrombin Heterozygotes.
Zhang H, Hu Y, Pan D, Xv Y, Shen W. Zhang H, et al. Front Genet. 2022 Apr 4;13:832582. doi: 10.3389/fgene.2022.832582. eCollection 2022. Front Genet. 2022. PMID: 35444682 Free PMC article. - Apolipoprotein (a)/Lipoprotein(a)-Induced Oxidative-Inflammatory _α_7-nAChR/p38 MAPK/IL-6/RhoA-GTP Signaling Axis and M1 Macrophage Polarization Modulate Inflammation-Associated Development of Coronary Artery Spasm.
Lin YK, Yeh CT, Kuo KT, Fong IH, Yadav VK, Kounis NG, Hu P, Hung MY. Lin YK, et al. Oxid Med Cell Longev. 2022 Jan 19;2022:9964689. doi: 10.1155/2022/9964689. eCollection 2022. Oxid Med Cell Longev. 2022. PMID: 35096275 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials