関: kringle

WordNet

territory over which rule or control is exercised; "his domain extended into Europe"; "he made it the law of the land" (同)demesne, land
(mathematics) the set of values of the independent variable for which a function is defined (同)domain of a function

PrepTutorEJDIC

(国の)領地,領土;(個人の)所有地 / (関心・活動などの)範囲,分野 / (個人・一族の)所有地 / (数学で)変域(関数の独立変数がとる値の集合)

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/10/25 17:09:51」(JST)

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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[edit]

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

References[edit]

^ 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.
^ 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.

External links[edit]

Kringle domain in PROSITE
KR domain entry in the SMART database

UpToDate Contents

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English Journal

Inhibition of mesothelioma cancer stem-like cells with adenovirus-mediated NK4 gene therapy.

Deng XB1, Xiao L2, Wu Y1, Jin F2, Mossman B3, Testa JR2, Xiao GH1,2.
International journal of cancer. Journal international du cancer.Int J Cancer.2015 Jul 15;137(2):481-90. doi: 10.1002/ijc.29391. Epub 2014 Dec 27.
Malignant mesothelioma (MM) is a highly invasive and chemoresistant malignancy induced by asbestos fibers. NK4, a hepatocyte growth factor antagonist and angiogenesis inhibitor, consists of the N-terminal hairpin domain and four kringle domains of the α-chain of hepatocyte growth factor. The therap
PMID 25501304

High-level expression, purification, and enzymatic characterization of truncated human plasminogen (Lys531-Asn791) in the methylotrophic yeast Pichia pastoris.

Liu R1,2, Zhao B3,4, Zhang Y5,6, Gu J7,8, Yu M9,10, Song H11,12,13, Yu M14,15, Mo W16,17.
BMC biotechnology.BMC Biotechnol.2015 Jun 9;15:50. doi: 10.1186/s12896-015-0179-z.
BACKGROUND: Plasmin is a serine protease that plays a critical role in fibrinolysis, which is a process that prevents blood clots from growing and becoming problematic. Recombinant human microplasminogen (rhμPlg) is a derivative of plasmin that solely consists of the catalytic domain of human plasm
PMID 26054637

Comparative study on the inhibition of plasmin and delta-plasmin via benzamidine derivatives.

Alves NJ1, Kline JA2.
Biochemical and biophysical research communications.Biochem Biophys Res Commun.2015 Feb 13;457(3):358-62. doi: 10.1016/j.bbrc.2014.12.117. Epub 2015 Jan 8.
The potent fibrinolytic enzyme, plasmin has numerous clinical applications for recannulizing vessels obstructed by thrombus. Despite its diminutive size, 91 kDa, success in the recombinant expression of this serine protease has been limited. For this reason, a truncated non-glycosylated plasmin vari
PMID 25576865

Japanese Journal

Three dimensional structure of full-length plasminogen

秋山正志,平井秀憲,宮田敏行
日本血栓止血学会誌 23(5), 516-519, 2012
NAID 130002077007

高リポ蛋白(a)血症とアポリポ蛋白(a)遺伝子多型 (特集脳卒中と遺伝子)

一瀬白帝
Brain and nerve 60(11), 1307-1317, 2008-11
NAID 40016342487

The Kringle Domain of Tissue-Type Plasminogen Activator Inhibits Extracellular Matrix-Induced Adhesion and Migration of Endothelial Cells

Lee Byung Hun,Kim Hyun-Kyung,Joe Young Ae
Bioscience, biotechnology, and biochemistry 72(9), 2303-2308, 2008-09-23
… The recombinant two-kringle domain of human tissue-type plasminogen activator (TK1-2) was found to inhibit angiogenesis and tumor growth. …
NAID 10027531784

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★リンクテーブル★

リンク元	「クリングル領域」「クリングルドメイン」
関連記事	「domain」「kringle」「domains」

「クリングル領域」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

	; Bovine prothrombin fragment 1 in complex with calcium and lysophosphatidylserine
Identifiers
Symbol	Kringle
Pfam	PF00051
InterPro	IPR000001
SMART	KR
PROSITE	PDOC00020
SCOP	1pk4
SUPERFAMILY	1pk4
OPM protein	1nl2
CDD	cd00108
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary