LEADER 03052nam  2200409z- 450 
001 9910346736903321
005 20231214132951.0
035   $a(CKB)4920000000094345
035   $a(oapen)https://directory.doabooks.org/handle/20.500.12854/52533
035   $a(EXLCZ)994920000000094345
100   $a20202102d2018      |y             0
101 0 $aeng
135   $aurmn|---annan
181   $ctxt$2rdacontent
182   $cc$2rdamedia
183   $acr$2rdacarrier
200 10$aMacromolecular Structure Underlying Recognition in Innate Immunity
210   $cFrontiers Media SA$d2018
215   $a1 electronic resource (151 p.)
225 1 $aFrontiers Research Topics
311   $a2-88945-527-0 
330   $aImmune molecules have evolved to distinguish ?self ?molecules from ?non-self?, ?altered self? and ?danger? molecules. Recognition is mediated via interactions between pattern recognition receptor molecules (PPRs) and their ligands, which include hydrophobic and electrostatic interactions between amino acid residues on the PPRs and uncharged or charged groups on amino acid residues, sugar rings or DNA/RNA molecules. Recognition in innate immunity range from cases (C1q, mannin-binding protein etc) where recognition is orchestrated by interaction between many ligands with one receptor molecule, and density of interaction is necessary for strong specific recognition, distinct from weak non-specific binding, and cases such as TLRs and NLRs where recognition involves complexation of single receptor and ligand, followed by oligomerisation of the receptor molecule. The majority of PPR molecules bind and recognise a wide variety of ligands, e.g TLR4 recognises LPS (gram negative bacteria), Lipotechoic acid (gram positive bacteria), heat shock protein hsp60, respiratory syncytial virus fusion protein etc, molecules that are structurally dissimilar to each other. This indicates considerable flexibility in their binding domains (amino acid residue variations) and modes (hydrophobic and charged, direct or mediated via an adaptor molecule). However, in many cases there is a dearth of structural and molecular data available, required to delineate the mechanism of ligand binding underlining recognition in pathogen receptors in innate immunity. Insights into requirements of conformation, charge, surface etc in the recognition and function of innate immunity receptors and their activation pathways, based on current data can suggest valuable avenues for future work.
610   $aHIV-1
610   $ahost-pathogen interactions
610   $azebrafish model system
610   $ainnate immunity
610   $aprotein-protein interaction
610   $acomplement
610   $amalaria
610   $apattern recognition
700   $aUttara SenGupta$4auth$01278728
702   $aMaha Ahmed Al-Mozaini$4auth
702   $aUday Kishore$4auth
906   $aBOOK
912   $a9910346736903321
996   $aMacromolecular Structure Underlying Recognition in Innate Immunity$93013805
997   $aUNINA