Cules C and D as part of the C interface. The binding cleft at the A?B contact is formed with the help of helices Aa2 and Ba2 together with N-terminal segments, Glu1?Glu14 of Naringin price molecule A(AN) and molecule B(BN).Structure of A Contact and Interactions of SAThe interface between molecules A and B represents an extended buried region with a buried surface area of approxi?mately 800 A2. The interface consists of a-helix a2 (residues, 118?134), N-terminal segment (residues, 1?4), loops (residues, 43?9) and (residues, 76?1) from each molecule (Figure 4). The important residues that form hydrogen bonds/ionic interactions and stabilize the A interface include Ser-8, Ile-9, Glu-14, Arg122 and Asn-126. The hydrogen bonds, Ser-8(A)NNNNNNNAsn??126(B)Od1 = 3.2 A, Ser-8(A)OcNNNNNNAsn-126(B)Od = 2.6 A are critical for dimerization and unique to CPGRP-S as the corresponding residues in HPGRP-S are Pro and Gly respectively.The C interface is formed with two CAL 120 site monomers through surfaces opposite to that of A contacts. The buried surface area ?at this interface was found to be of the order of 702 A2. This association is stabilized by six intermolecular hydrogen bonds and ?74 van der Waals contacts (distances #4.2 A). This interface consists of three important loops with residues, Tyr-592 Trp-66, Ala-942 Asn-99 and Arg-1472 Leu-153 from each molecule. The important residues at the interface are four prolines, Pro-96C, Pro151C, Pro-96D and Pro-151D. It may be noted here that the corresponding residues in HPGRP-S are His-99 and Arg-154 which are considered to be unfavorable for intermolecular stacking. This ligand binding cleft is situated at one end of the C interface having a glycan binding pocket inserted in molecule C. This ligand binding cleft consists of amino acid residues, Ser20, Thr-27, Trp-66, Asp-68, Arg-85 23977191 and Asn-99 from molecule C and a segment Gly-91?Asn-99 from molecule D (Figure 6B). Upon interaction with CPGRP-S, the glycan moiety of LPS is hooked into the glycan binding pocket in molecule C while the two hydrocarbon chains extend into two different directions whereby one is pushed into the binding space at the interface while the other one is aligned along the outer surface of molecule D. As a result of this several contacts are made by LPS with molecules C and D to produce a stable complex. The LPS molecule makes extensive contacts with protein molecules C and D with atleast two dozens of hydrogen bonds and a large number of van der Waals contacts. The residues that are involved in hydrogen bonded interactions are Trp-66, Arg-85, Lys-90, Gly-91, Ala-92, His-93 and Asn-99 from molecule C while residues, Thr-97, Asp-98, Val149 and Gln-150 are from molecule D. These interactions of LPS in the ternary complex are similar to those reported in the binaryWide Spectrum Antimicrobial Role of Camel PGRP-SFigure 6. The binding of SA and LPS to CPGRP-S, (A) A section of A contact showing a bound SA molecule in the cleft. The binding is essentially stabilized by van der Waals contacts. (B) A section of C contact showing a bound LPS molecule in the cleft. The binding is stabilized by several hydrogen bonds and a network of van der Waals contacts. doi:10.1371/journal.pone.0053756.gcomplex [9]. The positions and interactions of residues Lys-90 and Asn-99 were identical in both structures indicating the significance of their roles in the recognition of LPS.DiscussionSo far, crystal structures of PGRP-S have been determined from two species that include.Cules C and D as part of the C interface. The binding cleft at the A?B contact is formed with the help of helices Aa2 and Ba2 together with N-terminal segments, Glu1?Glu14 of molecule A(AN) and molecule B(BN).Structure of A Contact and Interactions of SAThe interface between molecules A and B represents an extended buried region with a buried surface area of approxi?mately 800 A2. The interface consists of a-helix a2 (residues, 118?134), N-terminal segment (residues, 1?4), loops (residues, 43?9) and (residues, 76?1) from each molecule (Figure 4). The important residues that form hydrogen bonds/ionic interactions and stabilize the A interface include Ser-8, Ile-9, Glu-14, Arg122 and Asn-126. The hydrogen bonds, Ser-8(A)NNNNNNNAsn??126(B)Od1 = 3.2 A, Ser-8(A)OcNNNNNNAsn-126(B)Od = 2.6 A are critical for dimerization and unique to CPGRP-S as the corresponding residues in HPGRP-S are Pro and Gly respectively.The C interface is formed with two monomers through surfaces opposite to that of A contacts. The buried surface area ?at this interface was found to be of the order of 702 A2. This association is stabilized by six intermolecular hydrogen bonds and ?74 van der Waals contacts (distances #4.2 A). This interface consists of three important loops with residues, Tyr-592 Trp-66, Ala-942 Asn-99 and Arg-1472 Leu-153 from each molecule. The important residues at the interface are four prolines, Pro-96C, Pro151C, Pro-96D and Pro-151D. It may be noted here that the corresponding residues in HPGRP-S are His-99 and Arg-154 which are considered to be unfavorable for intermolecular stacking. This ligand binding cleft is situated at one end of the C interface having a glycan binding pocket inserted in molecule C. This ligand binding cleft consists of amino acid residues, Ser20, Thr-27, Trp-66, Asp-68, Arg-85 23977191 and Asn-99 from molecule C and a segment Gly-91?Asn-99 from molecule D (Figure 6B). Upon interaction with CPGRP-S, the glycan moiety of LPS is hooked into the glycan binding pocket in molecule C while the two hydrocarbon chains extend into two different directions whereby one is pushed into the binding space at the interface while the other one is aligned along the outer surface of molecule D. As a result of this several contacts are made by LPS with molecules C and D to produce a stable complex. The LPS molecule makes extensive contacts with protein molecules C and D with atleast two dozens of hydrogen bonds and a large number of van der Waals contacts. The residues that are involved in hydrogen bonded interactions are Trp-66, Arg-85, Lys-90, Gly-91, Ala-92, His-93 and Asn-99 from molecule C while residues, Thr-97, Asp-98, Val149 and Gln-150 are from molecule D. These interactions of LPS in the ternary complex are similar to those reported in the binaryWide Spectrum Antimicrobial Role of Camel PGRP-SFigure 6. The binding of SA and LPS to CPGRP-S, (A) A section of A contact showing a bound SA molecule in the cleft. The binding is essentially stabilized by van der Waals contacts. (B) A section of C contact showing a bound LPS molecule in the cleft. The binding is stabilized by several hydrogen bonds and a network of van der Waals contacts. doi:10.1371/journal.pone.0053756.gcomplex [9]. The positions and interactions of residues Lys-90 and Asn-99 were identical in both structures indicating the significance of their roles in the recognition of LPS.DiscussionSo far, crystal structures of PGRP-S have been determined from two species that include.
