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| - | [[Image:1tpk.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1tpk| PDB=1tpk | SCENE= }} | | {{STRUCTURE_1tpk| PDB=1tpk | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION'''
| + | ===CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | The crystal structure of the kringle 2 domain of tissue plasminogen activator was determined and refined at a resolution of 2.43 A. The overall fold of the molecule is similar to that of prothrombin kringle 1 and plasminogen kringle 4; however, there are differences in the lysine binding pocket, and two looping regions, which include insertions in kringle 2, take on very different conformations. Based on a comparison of the overall structural homology between kringle 2 and kringle 4, a new sequence alignment for kringle domains is proposed that results in a division of kringle domains into two groups, consistent with their proposed evolutionary relation. The crystal structure shows a strong interaction between a lysine residue of one molecule and the lysine/fibrin binding pocket of a noncrystallographically related neighbor. This interaction represents a good model of a bound protein ligand and is the first such ligand that has been observed in a kringle binding pocket. The structure shows an intricate network of interactions both among the binding pocket residues and between binding pocket residues and the lysine ligand. A lysine side chain is identified as the positively charged group positioned to interact with the carboxylate of lysine and lysine analogue ligands. In addition, a chloride ion is located in the kringle-kringle interface and contributes to the observed interaction between kringle molecules. | + | The line below this paragraph, {{ABSTRACT_PUBMED_1310033}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1310033 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1310033}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Westbrook, M L.]] | | [[Category: Westbrook, M L.]] |
| | [[Category: Plasminogen activator]] | | [[Category: Plasminogen activator]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:13:29 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:09:35 2008'' |
Revision as of 10:09, 29 July 2008
Template:STRUCTURE 1tpk
CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 1310033
About this Structure
1TPK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution., de Vos AM, Ultsch MH, Kelley RF, Padmanabhan K, Tulinsky A, Westbrook ML, Kossiakoff AA, Biochemistry. 1992 Jan 14;31(1):270-9. PMID:1310033
Page seeded by OCA on Tue Jul 29 13:09:35 2008
