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Structural Basis of Interfacial Flexibility in Fibrin Oligomers.


ABSTRACT: Fibrin is a filamentous network made in blood to stem bleeding; it forms when fibrinogen is converted into fibrin monomers that self-associate into oligomers and then to polymers. To gather structural insights into fibrin formation and properties, we combined high-resolution atomic force microscopy of fibrin(ogen) oligomers and molecular modeling of crystal structures of fibrin(ogen) and its fragments. We provided a structural basis for the intermolecular flexibility of single-stranded fibrin(ogen) oligomers and identified a hinge region at the D:D inter-monomer junction. Following computational reconstruction of the missing portions, we recreated the full-atomic structure of double-stranded fibrin oligomers that was validated by quantitative comparison with the experimental images. We characterized previously unknown intermolecular binding contacts at the D:D and D:E:D interfaces, which drive oligomerization and reinforce the intra- and inter-strand connections in fibrin besides the known knob-hole bonds. The atomic models provide valuable insights into the submolecular mechanisms of fibrin polymerization.

SUBMITTER: Zhmurov A 

PROVIDER: S-EPMC5240993 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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Structural Basis of Interfacial Flexibility in Fibrin Oligomers.

Zhmurov Artem A   Protopopova Anna D AD   Litvinov Rustem I RI   Zhukov Pavel P   Mukhitov Alexander R AR   Weisel John W JW   Barsegov Valeri V  

Structure (London, England : 1993) 20160929 11


Fibrin is a filamentous network made in blood to stem bleeding; it forms when fibrinogen is converted into fibrin monomers that self-associate into oligomers and then to polymers. To gather structural insights into fibrin formation and properties, we combined high-resolution atomic force microscopy of fibrin(ogen) oligomers and molecular modeling of crystal structures of fibrin(ogen) and its fragments. We provided a structural basis for the intermolecular flexibility of single-stranded fibrin(og  ...[more]

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