Kringle domain

Pfam_box
Symbol = Kringle
Name =

---

width =
caption = Bovine prothrombin fragment 1 in complex with calcium and lysophosphatidylserine
Pfam= PF00051
InterPro= IPR000001
SMART= KR
PROSITE = PDOC00020
SCOP = 1pk4
TCDB =
OPM family=
OPM protein= 1nl2
PDB=PDB3|1pmlB:215-296 PDB3|1tpkA:215-296 PDB3|1pk2 :215-296PDB3|1kdu :70-151 PDB3|1urk :70-151 PDB3|5hpgB:481-560PDB3|1ceaB:103-181 PDB3|1ki0A:103-181 PDB3|1hpk :103-181PDB3|1cebB:103-181 PDB3|1pkr :103-181 PDB3|1hpj :103-181PDB3|1krn :377-454 PDB3|1pmkB:377-454 PDB3|1pk4 :377-454PDB3|2pk4 :377-454 PDB3|1kiv :4124-4201 PDB3|3kiv :4124-4201PDB3|4kiv :4124-4201 PDB3|1jfnA:3676-3753 PDB3|1i71A:3782-3859PDB3|1i5kB:185-262 PDB3|1b2iA:185-262 PDB3|1gmoF:128-206PDB3|1bhtB:128-206 PDB3|1gp9D:128-206 PDB3|1gmnB:128-206PDB3|1nk1B:128-206 PDB3|1nl1A:109-187 PDB3|2spt :109-187PDB3|1nl2A:109-187 PDB3|2pf1 :109-187 PDB3|1a0hD:214-292PDB3|2hppP:214-292 PDB3|2hpqP:213-291

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. The name Kringle comes from the Scandinavian pastry that these structures resemble.

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

External links

* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC00020 Kringle domain] in PROSITE
* [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=KR KR domain entry in the SMART database]