1tn3
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(New page: 200px<br /> <applet load="1tn3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tn3, resolution 2.0Å" /> '''THE C-TYPE LECTIN CA...)
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Revision as of 15:20, 29 October 2007
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THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN
Overview
Tetranectin (TN) is a C-type lectin involved in fibrinolysis, being the, only endogenous ligand known to bind specifically to the kringle 4 domain, of plasminogen. TN was originally isolated from plasma, but shows a wide, tissue distribution. Furthermore, TN has been found in the extracellular, matrix of certain human carcinomas, whereas none or little is present in, the corresponding normal tissue. The crystal structure of full-length, trimeric TN (2.8 A resolution) has recently been published [Nielsen et al., (1997). FEBS Lett. 412, 388-396]. The crystal structure of the, carbohydrate recognition domain (CRD) of human TN (TN3) has been, determined separately at 2.0 A resolution in order to obtain detailed, information on the two calcium binding sites. This information is, essential for ... [(full description)]
About this Structure
1TN3 is a [Single protein] structure of sequence from [Homo sapiens] with CA, SO4 and EOH as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structure of the C-type lectin carbohydrate recognition domain of human tetranectin., Kastrup JS, Nielsen BB, Rasmussen H, Holtet TL, Graversen JH, Etzerodt M, Thogersen HC, Larsen IK, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):757-66. PMID:9757090
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