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Kringle domain


Bovine prothrombin fragment 1 in complex with calcium and lysophosphatidylserine

Identifiers
Symbol	Kringle
Pfam	PF00051
InterPro	IPR000001
SMART	KR
SCOP	1pk4
OPM protein	1nl2
Available PDB structures: 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.

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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-disulphide 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. PMID 6373375.
^ 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. 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. PMID 3131537.
^ Patthy L (1985). "Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules". Cell 41 (3): 657-663. 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. PMID 1879523.

v • d • e Protein domains
BZIP - DED - Kringle - PH - SH2 - SH3 - zinc finger - FYVE - PX - ENTH - BAR - PDZ - CARD - SUN - TRIO - C1 - LIM - C2

Categories: Protein domains | Peripheral membrane proteins

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Kringle_domain". A list of authors is available in Wikipedia.