1tpk: Difference between revisions
New page: left|200px<br /> <applet load="1tpk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tpk, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1tpk. | [[Image:1tpk.jpg|left|200px]]<br /><applet load="1tpk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1tpk, resolution 2.4Å" /> | caption="1tpk, resolution 2.4Å" /> | ||
'''CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1TPK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1TPK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPK OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: plasminogen activator]] | [[Category: plasminogen activator]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:58:02 2008'' | ||
Revision as of 17:58, 15 February 2008
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CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Plasminogen activator deficiency OMIM:[173370]
About this StructureAbout this Structure
1TPK is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Hydrolase, with EC number and 3.4.21.73 3.4.21.68 and 3.4.21.73 Full crystallographic information is available from OCA.
ReferenceReference
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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