2jm2

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{{Seed}}
 
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[[Image:2jm2.png|left|200px]]
 
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==Structure of the N-terminal subdomain of insulin-like growth factor (IGF) binding protein-6 and its interactions with IGFs==
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The line below this paragraph, containing "STRUCTURE_2jm2", creates the "Structure Box" on the page.
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<StructureSection load='2jm2' size='340' side='right'caption='[[2jm2]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jm2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JM2 FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jm2 OCA], [https://pdbe.org/2jm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jm2 RCSB], [https://www.ebi.ac.uk/pdbsum/2jm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jm2 ProSAT]</span></td></tr>
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{{STRUCTURE_2jm2| PDB=2jm2 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IBP6_HUMAN IBP6_HUMAN] IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Insulin-like growth factor binding proteins (IGFBPs) modulate the activity and distribution of insulin-like growth factors (IGFs). IGFBP-6 differs from other IGFBPs in being a relatively specific inhibitor of IGF-II actions. Another distinctive feature of IGFBP-6 is its unique N-terminal disulfide linkages; the N-domains of IGFBPs 1-5 contain six disulfides and share a conserved GCGCC motif, but IGFBP-6 lacks the two adjacent cysteines in this motif, so its first three N-terminal disulfide linkages differ from those of the other IGFBPs. The contributions of the N- and C-domains of IGFBP-6 to its IGF binding properties and their structure-function relationships have been characterized in part, but the structure and function of the distinctive N-terminal subdomain of IGFBP-6 are unknown. Here we report the solution structure of a polypeptide corresponding to residues 1-45 of the N-terminal subdomain of IGFBP-6 (NN-BP-6). The extended structure of the N-terminal subdomain of IGFBP-6 is very different from that of the short two-stranded beta-sheet of the N-terminal subdomain of IGFBP-4 and, by implication, the other IGFBPs. NN-BP-6 contains a potential cation-binding motif; lanthanide ion binding was observed, but no significant interaction was found with physiologically relevant metal ions like calcium or magnesium. However, this subdomain of IGFBP-6 has a higher affinity for IGF-II than IGF-I, suggesting that it may contribute to the marked IGF-II binding preference of IGFBP-6. The extended structure and flexibility of this subdomain of IGFBP-6 could play a role in enhancing the rate of ligand association and thereby be significant in IGF recognition.
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===Structure of the N-terminal subdomain of insulin-like growth factor (IGF) binding protein-6 and its interactions with IGFs===
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The N-terminal subdomain of insulin-like growth factor (IGF) binding protein 6. Structure and interaction with IGFs.,Chandrashekaran IR, Yao S, Wang CC, Bansal PS, Alewood PF, Forbes BE, Wallace JC, Bach LA, Norton RS Biochemistry. 2007 Mar 20;46(11):3065-74. Epub 2007 Feb 17. PMID:17305365<ref>PMID:17305365</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2jm2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17305365}}, adds the Publication Abstract to the page
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*[[Insulin-like growth factor binding protein 3D structures|Insulin-like growth factor binding protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17305365 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17305365}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Homo sapiens]]
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM2 OCA].
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[[Category: Large Structures]]
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[[Category: Alewood PF]]
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==Reference==
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[[Category: Bach LA]]
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The N-terminal subdomain of insulin-like growth factor (IGF) binding protein 6. Structure and interaction with IGFs., Chandrashekaran IR, Yao S, Wang CC, Bansal PS, Alewood PF, Forbes BE, Wallace JC, Bach LA, Norton RS, Biochemistry. 2007 Mar 20;46(11):3065-74. Epub 2007 Feb 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17305365 17305365]
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[[Category: Bansal PS]]
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[[Category: Alewood, P F.]]
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[[Category: Chandrashekaran IR]]
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[[Category: Bach, L A.]]
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[[Category: Forbes BE]]
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[[Category: Bansal, P S.]]
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[[Category: Norton RS]]
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[[Category: Chandrashekaran, I R.]]
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[[Category: Wallace JC]]
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[[Category: Forbes, B E.]]
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[[Category: Wang CC]]
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[[Category: Norton, R S.]]
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[[Category: Yao S]]
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[[Category: Wallace, J C.]]
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[[Category: Wang, C C.]]
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[[Category: Yao, S.]]
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[[Category: Growth factor]]
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[[Category: Insulin like growth factor binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:31:05 2008''
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Current revision

Structure of the N-terminal subdomain of insulin-like growth factor (IGF) binding protein-6 and its interactions with IGFs

PDB ID 2jm2

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