Kringle domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1pmlB:215–296 1tpkA:215–296 1pk2 :215–296 1kdu :70–151 1urk :70–151 5hpgB:481–560 1ceaB:103–181 1ki0A:103–181 1hpk :103–181 1cebB:103–181 1pkr :103–181 1hpj :103–181 1krn :377–454 1pmkB:377–454 1pk4 :377–454 2pk4 :377–454 1kiv :4124–4201 3kiv :4124–4201 4kiv :4124–4201 1jfnA:3676–3753 1i71A:3782–3859 1i5kB:185–262 1b2iA:185–262 1gmoF:128–206 1bhtB:128–206 1gp9D:128–206 1gmnB:128–206 1nk1B:128–206 1nl1A:109–187 2spt :109–187 1nl2A:109–187 2pf1 :109–187 1a0hD:214–292 2hppP:214-292 2hpqP:213-291

	Bovine prothrombin fragment 1 in complex with calcium and lysophosphatidylserine
Identifiers
Symbol	Kringle
Pfam	PF00051
InterPro	IPR000001
SMART	KR
PROSITE	PDOC00020
SCOP2	1pk4 / SCOPe / SUPFAM
OPM protein	1nl2
CDD	cd00108
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1pmlB:215–296 1tpkA:215–296 1pk2 :215–296 1kdu :70–151 1urk :70–151 5hpgB:481–560 1ceaB:103–181 1ki0A:103–181 1hpk :103–181 1cebB:103–181 1pkr :103–181 1hpj :103–181 1krn :377–454 1pmkB:377–454 1pk4 :377–454 2pk4 :377–454 1kiv :4124–4201 3kiv :4124–4201 4kiv :4124–4201 1jfnA:3676–3753 1i71A:3782–3859 1i5kB:185–262 1b2iA:185–262 1gmoF:128–206 1bhtB:128–206 1gp9D:128–206 1gmnB:128–206 1nk1B:128–206 1nl1A:109–187 2spt :109–187 1nl2A:109–187 2pf1 :109–187 1a0hD:214–292 2hppP:214-292 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 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

^ 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. PMID 3886654.
^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ 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.
^ 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. doi:10.1007/BF02101155. PMID 3131537.
^ 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.
^ 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. {{cite journal}}: line feed character in |author= at position 18 (help)CS1 maint: multiple names: authors list (link)

External links

[PUB00002414-1] 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. PMID 3886654.

[PUB00001541-2] 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)

[PUB00003257-3] 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.

[PUB00003400-4] 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. doi:10.1007/BF02101155. PMID 3131537.

[PUB00000803-5] 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.

[PUB00001620-6] 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. {{cite journal}}: line feed character in |author= at position 18 (help)CS1 maint: multiple names: authors list (link)

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