1pml
From Proteopedia
(New page: 200px<br /> <applet load="1pml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pml, resolution 2.38Å" /> '''KRINGLE-KRINGLE INT...) |
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| - | [[Image:1pml.gif|left|200px]]<br /> | + | [[Image:1pml.gif|left|200px]]<br /><applet load="1pml" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1pml" size=" | + | |
caption="1pml, resolution 2.38Å" /> | caption="1pml, resolution 2.38Å" /> | ||
'''KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES'''<br /> | '''KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a monoclinic form of human plasminogen kringle 4 | + | The crystal structure of a monoclinic form of human plasminogen kringle 4 (PGK4) has been solved by molecular replacement using the orthorthombic structure as a model and it has been refined by restrained least-squares methods to an R factor of 16.4% at 2.25 A resolution. The X-PLOR structure of kringle 2 of tissue plasminogen activator (t-PAK2) has been refined further using PROFFT (R = 14.5% at 2.38 A resolution). The PGK4 structure has 2 and t-PAK2 has 3 independent molecules in the asymmetric unit. There are 5 different noncrystallographic symmetry "dimers" in PGK4. Three make extensive kringle-kringle interactions related by noncrystallographic 2(1) screw axes without blocking the lysine binding site. Such associations may occur in multikringle structures such as prothrombin, hepatocyte growth factor, plasminogen (PG), and apolipoprotein [a]. The t-PAK2 structure also has noncrystallographic screw symmetry (3(1)) and mimics fibrin binding mode by having lysine of one molecule interacting electrostatically with the lysine binding site of another kringle. This ligand-like binding interaction may be important in kringle-kringle interactions involving non-lysine binding kringles with lysine or pseudo-lysine binding sites. Electrostatic intermolecular interactions involving the lysine binding site are also found in the crystal structures of PGK1 and orthorhombic PGK4. Anions associate with the cationic centers of these and t-PAK2 that appear to be more than occasional components of lysine binding site regions. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PML 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/T-plasminogen_activator T-plasminogen activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.68 3.4.21.68] Full crystallographic information is available from [http:// | + | 1PML 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/T-plasminogen_activator T-plasminogen activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.68 3.4.21.68] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PML OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase(serine protease)]] | [[Category: hydrolase(serine protease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:18 2008'' |
Revision as of 12:30, 21 February 2008
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KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES
Contents |
Overview
The crystal structure of a monoclinic form of human plasminogen kringle 4 (PGK4) has been solved by molecular replacement using the orthorthombic structure as a model and it has been refined by restrained least-squares methods to an R factor of 16.4% at 2.25 A resolution. The X-PLOR structure of kringle 2 of tissue plasminogen activator (t-PAK2) has been refined further using PROFFT (R = 14.5% at 2.38 A resolution). The PGK4 structure has 2 and t-PAK2 has 3 independent molecules in the asymmetric unit. There are 5 different noncrystallographic symmetry "dimers" in PGK4. Three make extensive kringle-kringle interactions related by noncrystallographic 2(1) screw axes without blocking the lysine binding site. Such associations may occur in multikringle structures such as prothrombin, hepatocyte growth factor, plasminogen (PG), and apolipoprotein [a]. The t-PAK2 structure also has noncrystallographic screw symmetry (3(1)) and mimics fibrin binding mode by having lysine of one molecule interacting electrostatically with the lysine binding site of another kringle. This ligand-like binding interaction may be important in kringle-kringle interactions involving non-lysine binding kringles with lysine or pseudo-lysine binding sites. Electrostatic intermolecular interactions involving the lysine binding site are also found in the crystal structures of PGK1 and orthorhombic PGK4. Anions associate with the cationic centers of these and t-PAK2 that appear to be more than occasional components of lysine binding site regions.
Disease
Known disease associated with this structure: Plasminogen activator deficiency OMIM:[173370]
About this Structure
1PML is a Single protein structure of sequence from Homo sapiens with as ligand. Active as T-plasminogen activator, with EC number 3.4.21.68 Full crystallographic information is available from OCA.
Reference
Kringle-kringle interactions in multimer kringle structures., Padmanabhan K, Wu TP, Ravichandran KG, Tulinsky A, Protein Sci. 1994 Jun;3(6):898-910. PMID:8069221
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