1f0f: Difference between revisions

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-{{Seed}}
-[[Image:1f0f.png|left|200px]]
-<!--
+==Cecropin A(1-8)-magainin 2(1-12) gig deletion modification in dodecylphosphocholine micelles==
-The line below this paragraph, containing "STRUCTURE_1f0f", creates the "Structure Box" on the page.
+<StructureSection load='1f0f' size='340' side='right'caption='[[1f0f]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1f0f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F0F FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-{{STRUCTURE_1f0f|  PDB=1f0f  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0f OCA], [https://pdbe.org/1f0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f0f RCSB], [https://www.ebi.ac.uk/pdbsum/1f0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0f ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MAGA_XENLA MAGA_XENLA] Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.[https://www.uniprot.org/uniprot/CECA_HYACE CECA_HYACE] Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A 20-residue hybrid peptide CA(1-8)-MA(1-12) (CA-MA), incorporating residues 1-8 of cecropin A (CA) and residues 1-12 of magainin 2 (MA), has potent antimicrobial activity without toxicity against human erythrocytes. To investigate the effects of the Gly-Ile-Gly hinge sequence of CA-MA on the antibacterial and antitumor activities, two analogues in which the Gly-Ile-Gly sequence of CA-MA is either deleted (P1) or substituted with Pro (P2) were synthesized. The role of the tryptophan residue at position 2 of CA-MA on its antibiotic activity was also investigated using two analogues, in which the Trp2 residue of CA-MA is replaced with either Ala (P3) or Leu (P4). The tertiary structures of CA-MA, P2, and P4 in DPC micelles, as determined by NMR spectroscopy, have a short amphiphilic helix in the N-terminus and about three turns of alpha-helix in the C-terminus, with the flexible hinge region between them. The P1 analogue has an alpha-helix from Leu4 to Ala14 without any hinge structure. P1 has significantly decreased lytic activities against bacterial and tumor cells and PC/PS vesicles (3:1, w/w), and reduced pore-forming activity on lipid bilayers, while P2 retained effective lytic activities and pore-forming activity. The N-terminal region of P3 has a flexible structure without any specific secondary structure. The P3 modification caused a drastic decrease in the antibiotic activities, whereas P4, with the hydrophobic Leu side chain at position 2, retained its activities. On the basis of the tertiary structures, antibiotic activities, vesicle-disrupting activities, and pore-forming activities, the structure-function relationships can be summarized as follows. The partial insertion of the Trp2 of CA-MA into the membrane, as well as the electrostatic interactions between the positively charged Lys residues at the N-terminus of the CA-MA and the anionic phospholipid headgroups, leads to the primary binding to the cell membrane. Then, the flexibility or bending potential induced by the Gly-Ile-Gly hinge sequence or the Pro residue in the central part of the peptides may allow the alpha-helix in the C-terminus to span the lipid bilayer. These structural features are crucial for the potent antibiotic activities of CA-MA.
-===Cecropin A(1-8)-magainin 2(1-12) gig deletion modification in dodecylphosphocholine micelles===
+Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures.,Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y Biochemistry. 2000 Oct 3;39(39):11855-64. PMID:11009597<ref>PMID:11009597</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1f0f" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11009597}}, adds the Publication Abstract to the page
+*[[Magainin 2|Magainin 2]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11009597 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11009597}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Hyalophora cecropia]]
-F0F is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0F OCA].
+[[Category: Large Structures]]
+[[Category: Kim Y]]
-==Reference==
+[[Category: Lee S]]
-Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures., Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y, Biochemistry. 2000 Oct 3;39(39):11855-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11009597 11009597]
+[[Category: Oh D]]
-[[Category: Single protein]]
+[[Category: Shin SY]]
-[[Category: Kim, Y.]]
-[[Category: Lee, S.]]
-[[Category: Oh, D.]]
-[[Category: Shin, S Y.]]
-[[Category: Helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:17:47 2008''