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1ao2

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(New page: 200px<br /><applet load="1ao2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ao2" /> '''cobalt(III)-deglycopepleomycin determined by...)
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[[Image:1ao2.gif|left|200px]]<br /><applet load="1ao2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ao2" />
 
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'''cobalt(III)-deglycopepleomycin determined by NMR studies'''<br />
 
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==Overview==
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==cobalt(III)-deglycopepleomycin determined by NMR studies==
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Pepleomycin (PEP) is a metalloglycopeptide that has stronger anticancer, activity and less pulmonary toxicity than bleomycin (BLM). PEP, like BLM, exerts its action by binding to and degrading DNA in the presence of, oxygen and certain metals. Obtaining detailed structural information of, PEP and PEP-DNA complexes is crucial to understanding its anticancer, activity. The structures of two green forms of cobalt-PEP species, HO2-Co(III)-PEP (denoted CoPEP) and deglycosylated HO2-Co(III)-PEP, (denoted CodPEP) have been obtained by NOE restrained refinements. Earlier, studies of the related HO2-Co(III)-BLM A2 proposed that two chiral, conformers (form A or B) could exist with either the beta-aminoalanine, primary amine (A,NH2) or the mannose carbamoyl nitrogen (M,NH2) as the, axial ligand. Analysis of our NOESY data shows convincingly that form A is, the most probable conformer with the mannose carbamoyl M,NH2 and the, beta-aminoalanine primary amine A,NH2 as the axial ligands in CoPEP and, CodPEP, respectively. The NOE cross-peaks resulting from the interactions, between the N-terminus (i.e., the metal-binding domain) and the C-terminus, of CoPEP and CodPEP have similar patterns, suggesting that they both adopt, compact structures with the bithiazole group folded back over the, N-terminus.
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<StructureSection load='1ao2' size='340' side='right'caption='[[1ao2]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AO2 FirstGlance]. <br>
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1AO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with 3CO, PMY and PEO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AO2 OCA].
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</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=1ao2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ao2 OCA], [https://pdbe.org/1ao2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ao2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ao2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ao2 ProSAT]</span></td></tr>
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</table>
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==Reference==
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__TOC__
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Structures of cobalt(III)-pepleomycin and cobalt(III)-deglycopepleomycin (green forms) determined by NMR studies., Caceres-Cortes J, Sugiyama H, Ikudome K, Saito I, Wang AH, Eur J Biochem. 1997 Mar 15;244(3):818-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9108252 9108252]
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</StructureSection>
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Caceres-Cortes, J.]]
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[[Category: Caceres-Cortes J]]
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[[Category: Ikudome, K.]]
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[[Category: Ikudome K]]
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[[Category: Saito, I.]]
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[[Category: Saito I]]
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[[Category: Sugiyama, H.]]
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[[Category: Sugiyama H]]
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[[Category: Wang, A.H.J.]]
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[[Category: Wang AH-J]]
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[[Category: 3CO]]
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[[Category: PEO]]
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[[Category: PMY]]
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[[Category: anticancer drugs]]
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[[Category: bleomycin]]
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[[Category: deglycosylated pepleomycin]]
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[[Category: dna]]
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[[Category: peplomycin]]
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[[Category: solution structures]]
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[[Category: two-dimensional nmr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:07:36 2007''
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cobalt(III)-deglycopepleomycin determined by NMR studies

PDB ID 1ao2

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