2jm2

From Proteopedia

(Difference between revisions)

Revision as of 08:28, 14 June 2023

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

Structural highlights

2jm2 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chandrashekaran IR, Yao S, Wang CC, Bansal PS, Alewood PF, Forbes BE, Wallace JC, Bach LA, Norton RS. The N-terminal subdomain of insulin-like growth factor (IGF) binding protein 6. Structure and interaction with IGFs. Biochemistry. 2007 Mar 20;46(11):3065-74. Epub 2007 Feb 17. PMID:17305365 doi:http://dx.doi.org/10.1021/bi0619876

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jm2"

@@ Line 1: / Line 1: @@
 ==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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2jm2' size='340' side='right'caption='[[2jm2]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jm2]] is a 1 chain structure. 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>
+<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='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 ==
@@ Line 22: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Alewood, P F]]
+[[Category: Alewood PF]]
-[[Category: Bach, L A]]
+[[Category: Bach LA]]
-[[Category: Bansal, P S]]
+[[Category: Bansal PS]]
-[[Category: Chandrashekaran, I R]]
+[[Category: Chandrashekaran IR]]
-[[Category: Forbes, B E]]
+[[Category: Forbes BE]]
-[[Category: Norton, R S]]
+[[Category: Norton RS]]
-[[Category: Wallace, J C]]
+[[Category: Wallace JC]]
-[[Category: Wang, C C]]
+[[Category: Wang CC]]
-[[Category: Yao, S]]
+[[Category: Yao S]]
-[[Category: Growth factor]]
-[[Category: Hormone-growth factor complex]]
-[[Category: Insulin like growth factor binding protein]]

2jm2

From Proteopedia

Revision as of 08:28, 14 June 2023

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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