1pmk

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spinqualitylabelsall models 1pmk, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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 diseases associated with this structure: Conjunctivitis, ligneous OMIM:[173350], Plasminogen Tochigi disease OMIM:[173350], Plasminogen deficiency, types I and II OMIM:[173350], Thrombophilia, dysplasminogenemic OMIM:[173350]

About this Structure

1PMK is a Single protein structure of sequence from Homo sapiens. Active as Plasmin, with EC number 3.4.21.7 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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