Abstract
The fibrin B?125-135 site is involved in the lateral association of protofibrils
Highlights
Fibrinogen is a dimer, with each subunit of the molecule being formed by three polypeptide chains: Aα, Bβ and γ
MAb FnI-3c and its corresponding Fab-fragment inhibited the lateral association of fibrin protofibrils. We suggested that this inhibition was the result of blocking the monoclonal antibody (mAb) epitope, which coincided with the site involved in the protofibril lateral association [8]
Taking into consideration the data cited above, as well as our previous data on the inhibition of lateral association by fibrin-specific mAb FnI-3c, we investigated the localization of the mAb FnI-3c epitope at Bβ119-133, including the stage of fibrin polymerization when the epitope exposure takes place, the structure of the hinge itself, and, the functional role of the structural rearrangement in the hinge locus of the coiled-coil region of the fibrin molecule
Summary
Fibrinogen is a dimer, with each subunit of the molecule being formed by three polypeptide chains: Aα, Bβ and γ. The molecule consists of a central E, two peripheral D, and two extended αC regions [1]. The central E-region consisting of (Aα1-104, Bβ1133, γ1-72) is connected to the two peripheral Dregions (Aα105-219, Bβ134-461, γ73-411) by two long flexible coiled-coil connectors (Aα48-161, Bβ79-193, γ23-135). The N-terminal parts of the connectors (Aα48-104, Bβ79-133, γ23-62) belong to the E region and the C-terminal parts (Aα105-161, Bβ134-193, γ63-135) to the D regions. A hinge locus (α99-110, β130-155, γ70-100) is located in the middle part of the coiled-coil region [2, 3]. The extended αC regions (Aα220-610) consist of unfolded flexible segments (Aα220-391) and more structured αC-domains (Aα392-610)
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
