Evolutionary analysis reveals collective properties and specificity in the C‐type lectin and lectin‐like domain superfamily

  title={Evolutionary analysis reveals collective properties and specificity in the C‐type lectin and lectin‐like domain superfamily},
  author={Sharon Ebner and Nathan Sharon and Nir Ben-Tal},
  journal={Proteins: Structure},
Members of the C‐type lectin/C‐type lectin‐like domain (CTL/CTLD) superfamily share a common fold and are involved in a variety of functions, such as generalized defense mechanisms against foreign agents, discrimination between healthy and pathogen‐infected cells, and endocytosis and blood coagulation. In this work we used ConSurf, a computer program recently developed in our lab, to perform an evolutionary analysis of this superfamily in order to further identify characteristics of all or part… 

C-type lectin protein isoforms of Macrovipera lebetina: cDNA cloning and genetic diversity.

Molecular cloning and expression of a C-type lectin gene from Venerupis philippinarum

A C-type lectin gene (denoted as VpCTL) was identified from Venerupis philippinarum by expressed sequence tag and rapid amplification of cDNA ends approaches and the deduced amino acid sequence of V pCTL shared high similarity with C- type lectins from other species.

On the quaternary structure of a C-type lectin from Bothrops jararacussu venom--BJ-32 (BjcuL).

cDNA cloning and expression of a collectin from red-spotted grouper (Epinephelus akaara)

The complete cDNA of a C-type lectin (EALec1) from Epinephelus akaara is obtained and inserted into an expression vector (pET-28a) for transformation into the BL21 engineering bacteria.

Prediction of a Putative Functional Region in the Human Bax Protein by Computational Analysis

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C-type Lectin CD209L/L-SIGN and CD209/DC-SIGN: Cell Adhesion Molecules Turned to Pathogen Recognition Receptors

Recent advances in the cellular and biochemical characterization of CD209 and CD209L and their roles in viral uptake have important implications in understanding the host–pathogen interaction, the viral pathobiology and driving vaccine development of SARS-CoV-2.



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New structural insights into lectin-type proteins of the immune system.

C-type lectin-like domains.

  • K. Drickamer
  • Biology
    Current opinion in structural biology
  • 1999

Structure of the C-type lectin carbohydrate recognition domain of human tetranectin.

The crystal structure of the carbohydrate recognition domain (CRD) of human TN (TN3) has been determined separately at 2.0 A resolution in order to obtain detailed information on the two calcium binding sites, essential for the elucidation of the specificity of TN towards oligosaccharides.

ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information.

A novel methodology based on evolutionary relations among proteins as revealed by inferred phylogenetic trees is presented, and its capabilities for mapping binding sites in SH2 and PTB signaling domains are demonstrated.

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Bothrojaracin is a potent and selective thrombin inhibitor that has been isolated from the venom of Bothrops jararaca and binds to both anion-binding exosites 1 and 2 resulting in a potent inhibition ofThrombin activity towards fibrinogen and platelets.

Automated structure-based prediction of functional sites in proteins: applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking.

It is shown that one can employ a strategy that uses a structure-based prediction of protein functional sites to assess the reliability of functional inheritance and automated and benchmarked a method based on the evolutionary trace approach.

Cloning of subunits of convulxin, a collagen-like platelet-aggregating protein from Crotalus durissus terrificus venom.

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