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[[Image:2jm2.gif|left|200px]]
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{{STRUCTURE_2jm2|  PDB=2jm2  |  SCENE=  }}
'''Structure of the N-terminal subdomain of insulin-like growth factor (IGF) binding protein-6 and its interactions with IGFs'''


==Structure of the N-terminal subdomain of insulin-like growth factor (IGF) binding protein-6 and its interactions with IGFs==
<StructureSection load='2jm2' size='340' side='right'caption='[[2jm2]]' scene=''>
== Structural highlights ==
<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>
</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='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>
</table>
== Function ==
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM2 OCA].
</div>
<div class="pdbe-citations 2jm2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Insulin-like growth factor binding protein 3D structures|Insulin-like growth factor binding protein 3D structures]]
[[Category: Alewood, P F.]]
== References ==
[[Category: Bach, L A.]]
<references/>
[[Category: Bansal, P S.]]
__TOC__
[[Category: Chandrashekaran, I R.]]
</StructureSection>
[[Category: Forbes, B E.]]
[[Category: Homo sapiens]]
[[Category: Norton, R S.]]
[[Category: Large Structures]]
[[Category: Wallace, J C.]]
[[Category: Alewood PF]]
[[Category: Wang, C C.]]
[[Category: Bach LA]]
[[Category: Yao, S.]]
[[Category: Bansal PS]]
[[Category: Growth factor]]
[[Category: Chandrashekaran IR]]
[[Category: Insulin like growth factor binding protein]]
[[Category: Forbes BE]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:00:54 2008''
[[Category: Norton RS]]
[[Category: Wallace JC]]
[[Category: Wang CC]]
[[Category: Yao S]]
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