From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2jm2.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2jm2.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2jm2| PDB=2jm2 | SCENE= }} | | {{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=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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 line below this paragraph, {{ABSTRACT_PUBMED_17305365}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17305365 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17305365}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM2 OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM2 OCA]. |
| | | | |
| | ==Reference== | | ==Reference== |
| Line 31: |
Line 35: |
| | [[Category: Growth factor]] | | [[Category: Growth factor]] |
| | [[Category: Insulin like growth factor binding protein]] | | [[Category: Insulin like growth factor binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:00:54 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:31:05 2008'' |
Revision as of 09:31, 28 July 2008
Template:STRUCTURE 2jm2
Structure of the N-terminal subdomain of insulin-like growth factor (IGF) binding protein-6 and its interactions with IGFs
Template:ABSTRACT PUBMED 17305365
About this Structure
Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Mon Jul 28 12:31:05 2008
