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| - | [[Image:1pmk.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1pmk| PDB=1pmk | SCENE= }} | | {{STRUCTURE_1pmk| PDB=1pmk | SCENE= }} |
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| - | '''KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES'''
| + | ===KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8069221}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8069221 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8069221}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Padmanabhan, K.]] | | [[Category: Padmanabhan, K.]] |
| | [[Category: Tulinsky, A.]] | | [[Category: Tulinsky, A.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:15:09 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:53:43 2008'' |
Revision as of 13:53, 28 July 2008
Template:STRUCTURE 1pmk
KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES
Template:ABSTRACT PUBMED 8069221
About this Structure
1PMK is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Mon Jul 28 16:53:43 2008
