NDLI: Kringle-kringle interactions in multimer kringle structures.

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Kringle-kringle interactions in multimer kringle structures.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Padmanabhan, K. Ravichandran, K. G. Tulinsky, A. Wu, T. P.
Description	Author Affiliation: Padmanabhan K ( Department of Chemistry, Michigan State University, East Lansing 48824.)
Abstract	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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Kringles Plasminogen Chemistry Amino Acid Sequence Binding Sites Chemical Phenomena Chemistry, Physical Crystallization Crystallography, X-ray Electrochemistry Lysine Metabolism Macromolecular Substances Molecular Sequence Data Protein Conformation Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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