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Cited by 45Coagulation, Bradykinin, Polyphosphates, and AngioedemaComplement system in diseasesEnzyme Structure and Function

The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.

High Molecular Weight Kininogen: A Review of the Structural Literature

Open access
Ponczek, Michał B.·2021·International Journal of Molecular Sciences
DOI 10.3390/ijms222413370PMC PMC8706920

Published version of a preprint

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Abstract

Kininogens are multidomain glycoproteins found in the blood of most vertebrates. High molecular weight kininogen demonstrate both carrier and co-factor activity as part of the intrinsic pathway of coagulation, leading to thrombin generation. Kininogens are the source of the vasoactive nonapeptide bradykinin. To date, attempts to crystallize kininogen have failed, and very little is known about the shape of kininogen at an atomic level. New advancements in the field of cryo-electron microscopy (cryoEM) have enabled researchers to crack the structure of proteins that has been refractory to traditional crystallography techniques. High molecular weight kininogen is a good candidate for structural investigation by cryoEM. The goal of this review is to summarize the findings of kininogen structural studies.

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Crossref · 10.3390/ijms222413370

Cites

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Figures

Figure 1 Blood coagulation cascade. Roman numerals denote individual coagulation factors, the letter “a” stands for the active form, other abbreviations are as in the text.
Figure 1 Blood coagulation cascade. Roman numerals denote individual coagulation factors, the letter “a” stands for the active form, other abbreviations are as in the text.CC BY · PubMed Central
Figure 2 (A) Human plasma kininogen showing alternative splicing products of KNG1 gene messenger RNA–HK and LK. Both forms of protein have similar D1, D2, D3, and D4 domains, but different D5 domains. Domain 6 is absent in LK and the molecular weight of this form is lower than that of HK. (B) Human HK amino acid sequence according to UniProt P01042 with the indication of domains. N-terminus and C-terminus marked by corresponding letters. Disulfide (SS) bonds between the respective domains are marked.
Figure 2 (A) Human plasma kininogen showing alternative splicing products of KNG1 gene messenger RNA–HK and LK. Both forms of protein have similar D1, D2, D3, and D4 domains, but different D5 domains. Domain 6 is absent in LK and the molecular weight of this form is lower than that of HK. (B) Human HK amino acid sequence according to UniProt P01042 with the indication of domains. N-terminus and C-terminus marked by corresponding letters. Disulfide (SS) bonds between the respective domains are marked.CC BY · PubMed Central
Figure 3 AlphaFold prediction of human HK. Colors of domains according to Figure 2. The structure contains a signal peptide colored brown. The figure was prepared in UCSF Chimera 1.15 based on downloaded AlPhaFold PDB coordinates (accessed date 29 October 2021) [50,51].
Figure 3 AlphaFold prediction of human HK. Colors of domains according to Figure 2. The structure contains a signal peptide colored brown. The figure was prepared in UCSF Chimera 1.15 based on downloaded AlPhaFold PDB coordinates (accessed date 29 October 2021) [50,51].CC BY · PubMed Central

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Cites

Research works printed but not linked: 1

  1. Waterhouse, 2004, UCSF Chimera—A visualization system for exploratory research and analysis, J. Biol. Chem., 25, 1605

Metadata

Authors
Ponczek, M. B.
Affiliations
Department of General Biochemistry, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska 141/143, 90-236 Lodz, Poland
ORCID
Ponczek, Michał B.
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2021-12-13
Volume
22
Issue
24
Pages
13370
ISSN
1422-0067 (ISSN-L)
DOI
10.3390/ijms222413370
PMC
PMC8706920
OpenAlex
W4200368767
Cited by
45
References
56
Citations by year
2026: 11 · 2025: 10 · 2024: 3 · 2023: 15 · 2022: 6
FWCI
0.85
Type
journal article
Language
en
Open access
Licence
Locations
  • International Journal of Molecular Sciences (publishedVersion, cc-by)
  • Preprints.org (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Saint Louis University
  • National Institutes of Health
  • University of California, San Francisco
  • National Center for Research Resources (P41RR001081)
Topics
  • Health Sciences › Medicine › Hematology › Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Life Sciences › Immunology and Microbiology › Immunology › Complement system in diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
high molecular weight kininogen, intrinsic coagulation pathway, thrombin generation, bradykinin, protein structure, cryo-electron microscopy
MeSH terms
Animals, Bradykinin, Humans, Kallikreins, Kininogens, Structure-Activity Relationship, Kininogen, High-Molecular-Weight, Cryoelectron Microscopy

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