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| | {{STRUCTURE_1tn3| PDB=1tn3 | SCENE= }} | | {{STRUCTURE_1tn3| PDB=1tn3 | SCENE= }} |
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| - | '''THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN'''
| + | ===THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN=== |
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| - | ==Overview==
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| - | 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 the elucidation of the specificity of TN towards oligosaccharides. TN3 crystallizes as a dimer, whereas it appears as a monomer in solution. The overall fold of TN3 is similar to other known CRDs. Each monomer is built of two distinct regions, one region consisting of six beta-strands and two alpha-helices, and the other region is composed of four loops harboring two calcium ions. The calcium ion at site 1 forms an eightfold coordinated complex and has Asp116, Glu120, Gly147, Glu150, Asn151, and one water molecule as ligands. The calcium ion at site 2, which is believed to be involved in recognition and binding of oligosaccharides, is sevenfold coordinated with ligands Gln143, Asp145, Glu150, Asp165, and two water molecules. One sulfate ion has been located at the surface of TN3, forming contacts to Glu120, Lys148, Asn106 of a symmetry-related molecule, and to an ethanol molecule.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9757090}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9757090 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9757090}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Plasminogen binding]] | | [[Category: Plasminogen binding]] |
| | [[Category: Tetranectin]] | | [[Category: Tetranectin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:08:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:55:29 2008'' |
Revision as of 10:55, 28 July 2008
Template:STRUCTURE 1tn3
THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN
Template:ABSTRACT PUBMED 9757090
About this Structure
1TN3 is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Mon Jul 28 13:55:29 2008
