1tpk
From Proteopedia
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| - | [[Image:1tpk.jpg|left|200px]] | + | [[Image:1tpk.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1tpk |SIZE=350|CAPTION= <scene name='initialview01'>1tpk</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.68 and 3.4.21.73 3.4.21.68 and 3.4.21.73] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TPK is a [ | + | 1TPK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPK OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1310033 1310033] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
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[[Category: plasminogen activator]] | [[Category: plasminogen activator]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:21:28 2008'' |
Revision as of 12:21, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Hydrolase, with EC number and 3.4.21.73 3.4.21.68 and 3.4.21.73 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION
Contents |
Overview
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.
Disease
Known disease associated with this structure: Plasminogen activator deficiency OMIM:[173370]
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
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