Kringle_domain

Kringle domain

Kringle domain

Autonomous protein domains

Kringle domains are autonomous protein domains that fold into large loops stabilized by 3 disulfide linkages. These are important in protein–protein interactions with blood coagulation factors. Their name refers to the Kringle, a Scandinavian pastry which they somewhat resemble.

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Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein(a).

Kringles are found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity.[1][2][3] Kringle domains[4][5][6] are characterised by a triple loop, 3-disulfide bridge structure, whose conformation is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. They are found in a varying number of copies in some plasma proteins including prothrombin and urokinase-type plasminogen activator, which are serine proteases belonging to MEROPS peptidase family S1A.

Human proteins containing this domain

ATF; F12; F2; HABP2; HGF; HGFAC; KREMEN1; KREMEN2; LPA; LPAL2; MST1; PIK3IP1; PLAT; PLAU; PLG; PRSS12; ROR1; ROR2;

References

  1. [1]
    Fujikawa K, McMullen BA (1985). "Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)". J. Biol. Chem. 260 (9): 5328–5341. doi:10.1016/S0021-9258(18)89026-3. PMID 3886654.
  2. [2]
    Patthy L, Trexler M, Banyai L, Varadi A, Vali Z (1984). "Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases". FEBS Lett. 171 (1): 131–136. doi:10.1016/0014-5793(84)80473-1. PMID 6373375. S2CID 12669742.
  3. [3]
    Atkinson RA, Williams RJ (1990). "Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry". J. Mol. Biol. 212 (3): 541–552. doi:10.1016/0022-2836(90)90330-O. PMID 2157850.
  4. [4]
    Castellino FJ, Beals JM (1987). "The genetic relationships between the kringle domains of human plasminogen, prothrombin, tissue plasminogen activator, urokinase, and coagulation factor XII". J. Mol. Evol. 26 (4): 358–369. Bibcode:1987JMolE..26..358C. doi:10.1007/BF02101155. PMID 3131537. S2CID 22249781.
  5. [5]
    Patthy L (1985). "Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules". Cell. 41 (3): 657–663. doi:10.1016/S0092-8674(85)80046-5. PMID 3891096. S2CID 32104232.
  6. [6]
    Takahashi K, Ikeo K, Gojobori T (1991). "Evolutionary origin of numerous kringles in human and simian apolipoprotein(a)". FEBS Lett. 287 (1): 146–148. doi:10.1016/0014-5793(91)80036-3. PMID 1879523. S2CID 13366195.
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