2,585 research outputs found

    The structures of secretory and dimeric immunoglobulin A

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    Secretory (S) Immunoglobulin (Ig) A is the predominant mucosal antibody, which binds pathogens and commensal microbes. SIgA is a polymeric antibody, typically containing two copies of IgA that assemble with one joining-chain (JC) to form dimeric (d) IgA that is bound by the polymeric Ig-receptor ectodomain, called secretory component (SC). Here, we report the cryo-electron microscopy structures of murine SIgA and dIgA. Structures reveal two IgAs conjoined through four heavy-chain tailpieces and the JC that together form a β-sandwich-like fold. The two IgAs are bent and tilted with respect to each other, forming distinct concave and convex surfaces. In SIgA, SC is bound to one face, asymmetrically contacting both IgAs and JC. The bent and tilted arrangement of complex components limits the possible positions of both sets of antigen-binding fragments (Fabs) and preserves steric accessibility to receptor-binding sites, likely influencing antigen binding and effector functions

    Towards an Iterative Algorithm for the Optimal Boundary Coverage of a 3D Environment

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    This paper presents a new optimal algorithm for locating a set of sensors in 3D able to see the boundaries of a polyhedral environment. Our approach is iterative and is based on a lower bound on the sensors' number and on a restriction of the original problem requiring each face to be observed in its entirety by at least one sensor. The lower bound allows evaluating the quality of the solution obtained at each step, and halting the algorithm if the solution is satisfactory. The algorithm asymptotically converges to the optimal solution of the unrestricted problem if the faces are subdivided into smaller part

    The structures of secretory and dimeric immunoglobulin A

    Get PDF
    Secretory (S) Immunoglobulin (Ig) A is the predominant mucosal antibody, which binds pathogens and commensal microbes. SIgA is a polymeric antibody, typically containing two copies of IgA that assemble with one joining-chain (JC) to form dimeric (d) IgA that is bound by the polymeric Ig-receptor ectodomain, called secretory component (SC). Here, we report the cryo-electron microscopy structures of murine SIgA and dIgA. Structures reveal two IgAs conjoined through four heavy-chain tailpieces and the JC that together form a β-sandwich-like fold. The two IgAs are bent and tilted with respect to each other, forming distinct concave and convex surfaces. In SIgA, SC is bound to one face, asymmetrically contacting both IgAs and JC. The bent and tilted arrangement of complex components limits the possible positions of both sets of antigen-binding fragments (Fabs) and preserves steric accessibility to receptor-binding sites, likely influencing antigen binding and effector functions

    3-D Shape Matching for Face Analysis and Recognition

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    The aims of this paper are to introduce a 3-D shape matching scheme for automatic face recognition and to demonstrate its invariance to pose and facial expressions. The core of this scheme lies on the combination of non-rigid deformation registration and statistical shape modelling. While the former matches 3-D faces regardless of facial expression variations, the latter provides a low-dimensional feature vector that describes the deformation after the shape matching process, thereby enabling robust identification of 3-D faces. In order to assist establishment of accurate dense point correspondences, an isometric embedding shape representation is introduced, which is able to transform 3-D faces to a canonical form that retains the intrinsic geometric structure and achieve shape alignment of 3-D faces independent from individual’s facial expression. The feasibility and effectiveness of the proposed method was investigated using standard publicly available Gavab and BU-3DFE databases, which contain faces expressions and pose variations. The performance of the system was compared with the existing benchmark approaches and it demonstrates that the proposed scheme provides a competitive solution for the face recognition task with real-world practicality
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