1ao4

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[[Image:1ao4.gif|left|200px]]
[[Image:1ao4.gif|left|200px]]
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{{Structure
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|PDB= 1ao4 |SIZE=350|CAPTION= <scene name='initialview01'>1ao4</scene>
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The line below this paragraph, containing "STRUCTURE_1ao4", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene>, <scene name='pdbligand=3FM:3-O-FORMAMIDO-ALPHA-D-MANNOPYRANOSIDE'>3FM</scene>, <scene name='pdbligand=GUP:BETA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=PMY:AGLYCON+OF+PEPLOMYCIN'>PMY</scene>
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{{STRUCTURE_1ao4| PDB=1ao4 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ao4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ao4 OCA], [http://www.ebi.ac.uk/pdbsum/1ao4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ao4 RCSB]</span>
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'''COBALT(III)-PEPLOMYCIN COMPLEX DETERMINED BY NMR STUDIES'''
'''COBALT(III)-PEPLOMYCIN COMPLEX DETERMINED BY NMR STUDIES'''
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==About this Structure==
==About this Structure==
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1AO4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AO4 OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AO4 OCA].
==Reference==
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/9108252 9108252]
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://www.ncbi.nlm.nih.gov/pubmed/9108252 9108252]
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[[Category: Protein complex]]
 
[[Category: Caceres-Cortes, J.]]
[[Category: Caceres-Cortes, J.]]
[[Category: Ikudome, K.]]
[[Category: Ikudome, K.]]
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[[Category: Sugiyama, H.]]
[[Category: Sugiyama, H.]]
[[Category: Wang, A H.J.]]
[[Category: Wang, A H.J.]]
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[[Category: anticancer drug]]
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[[Category: Anticancer drug]]
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[[Category: bleomycin]]
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[[Category: Bleomycin]]
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[[Category: dna]]
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[[Category: Dna]]
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[[Category: pepleomycin]]
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[[Category: Pepleomycin]]
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[[Category: peplomycin]]
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[[Category: Peplomycin]]
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[[Category: solution structure]]
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[[Category: Solution structure]]
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[[Category: two-dimensional nmr]]
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[[Category: Two-dimensional nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:29:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:44:11 2008''
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Revision as of 07:30, 2 May 2008

Template:STRUCTURE 1ao4

COBALT(III)-PEPLOMYCIN COMPLEX DETERMINED BY NMR STUDIES


Overview

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.

About this Structure

Full crystallographic information is available from OCA.

Reference

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:9108252 Page seeded by OCA on Fri May 2 10:29:58 2008

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