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[[Image:1kb7.jpg|left|200px]]
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{{STRUCTURE_1kb7|  PDB=1kb7  |  SCENE=  }}
'''A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN'''


==A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN==
<StructureSection load='1kb7' size='340' side='right'caption='[[1kb7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kb7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KB7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kb7 OCA], [https://pdbe.org/1kb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kb7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kb7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FMK7_PSEAI FMK7_PSEAI]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structures of peptide antigens from the receptor binding domains of Pseudomonas aeruginosa strains PAO and KB7 have been determined using two-dimensional 1H NMR techniques. Ensembles of solution conformations for the trans forms of these 17-residue disulfide-bridged peptides have been generated using a simulated annealing procedure in conjunction with distance and torsion angle restraints derived from NMR data. Comparison of the NMR-derived solution structures of the PAO and KB7 peptides, with that previously determined (McInnes et al., 1993) and herein refined for the PAK peptide reveals a common structural motif. All three peptide structures contain a type I beta-turn in the conserved sequence Asp134-X-X-Phe137 and a type II beta-turn in the conserved sequence Pro139-X-Gly-Cys142. However, the overall folds of the three peptides differ as well as the disposition of the side chains comprising the hydrophobic pockets. The similarities and differences between the structures of the three strains which bind to a common cell surface receptor are discussed in light of their contributions to synthetic vaccine design.


==Overview==
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.,Campbell AP, McInnes C, Hodges RS, Sykes BD Biochemistry. 1995 Dec 19;34(50):16255-68. PMID:8845350<ref>PMID:8845350</ref>
The solution structures of peptide antigens from the receptor binding domains of Pseudomonas aeruginosa strains PAO and KB7 have been determined using two-dimensional 1H NMR techniques. Ensembles of solution conformations for the trans forms of these 17-residue disulfide-bridged peptides have been generated using a simulated annealing procedure in conjunction with distance and torsion angle restraints derived from NMR data. Comparison of the NMR-derived solution structures of the PAO and KB7 peptides, with that previously determined (McInnes et al., 1993) and herein refined for the PAK peptide reveals a common structural motif. All three peptide structures contain a type I beta-turn in the conserved sequence Asp134-X-X-Phe137 and a type II beta-turn in the conserved sequence Pro139-X-Gly-Cys142. However, the overall folds of the three peptides differ as well as the disposition of the side chains comprising the hydrophobic pockets. The similarities and differences between the structures of the three strains which bind to a common cell surface receptor are discussed in light of their contributions to synthetic vaccine design.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1KB7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KB7 OCA].
</div>
<div class="pdbe-citations 1kb7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design., Campbell AP, McInnes C, Hodges RS, Sykes BD, Biochemistry. 1995 Dec 19;34(50):16255-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8845350 8845350]
*[[Pilin 3D structures|Pilin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Campbell AP]]
[[Category: Campbell, A P.]]
[[Category: Hodges RS]]
[[Category: Hodges, R S.]]
[[Category: Mcinnes C]]
[[Category: Mcinnes, C.]]
[[Category: Sykes BD]]
[[Category: Sykes, B D.]]
[[Category: Fimbrial protein]]
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