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| | {{STRUCTURE_3lri| PDB=3lri | SCENE= }} | | {{STRUCTURE_3lri| PDB=3lri | SCENE= }} |
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| - | '''SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF HUMAN LONG-[ARG3]INSULIN-LIKE GROWTH FACTOR 1'''
| + | ===SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF HUMAN LONG-[ARG3]INSULIN-LIKE GROWTH FACTOR 1=== |
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| - | ==Overview==
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| - | Long-[Arg(3)]insulin-like growth factor-I (IGF-I) is a potent analog of insulin-like growth factor-I that has been modified by a Glu(3) --> Arg mutation and a 13-amino acid extension appended to the N terminus. We have determined the solution structure of (15)N-labeled Long-[Arg(3)]-IGF-I using high resolution NMR and restrained molecular dynamics techniques to a precision of 0.82 +/- 0.28 A root mean square deviation for the backbone heavy atoms in the three alpha-helices and 3.5 +/- 0.9 A root mean square deviation for all backbone heavy atoms excluding the 8 N-terminal residues and the 8 C-terminal eight residues. Overall, the structure of the IGF-I domain is consistent with earlier studies of IGF-I with some minor changes remote from the N terminus. The major variations in the structure, compared with IGF-I, occur at the N terminus with a substantial reorientation of the N-terminal three residues of the IGF-I domain. These results are interpreted in terms of the lower binding affinity for insulin-like growth factor-binding proteins. The backbone dynamics of Long-[Arg(3)]IGF-I were investigated using (15)N nuclear spin relaxation and the heteronuclear nuclear Overhauser enhancement (NOE). There is a considerable degree of flexibility in Long-[Arg(3)]IGF-I, even in the alpha-helices, as indicated by an average ((1)H)(15)N NOE of 0.55 for the regions. The largest heteronuclear NOEs are observed in the helical regions, lower heteronuclear NOEs are observed in the C-domain loop separating helix 1 from helix 2, and negative heteronuclear NOEs are observed in the N-terminal extension and at the C terminus. Despite these data indicating conformational flexibility for the N-terminal extension, slow amide proton exchange was observed for some residues in this region, suggesting some transitory structure does exist, possibly a molten helix. A certain degree of flexibility may be necessary in all insulin-like growth factors to enable association with various receptors and binding proteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10744677}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10744677 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10744677}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 3LRI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRI OCA]. | + | 3LRI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRI OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Nmr]] | | [[Category: Nmr]] |
| | [[Category: Protein structure]] | | [[Category: Protein structure]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:06:04 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:53:50 2008'' |
Revision as of 09:53, 3 July 2008
Template:STRUCTURE 3lri
SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF HUMAN LONG-[ARG3]INSULIN-LIKE GROWTH FACTOR 1
Template:ABSTRACT PUBMED 10744677
About this Structure
3LRI is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
Solution structure and backbone dynamics of long-[Arg(3)]insulin-like growth factor-I., Laajoki LG, Francis GL, Wallace JC, Carver JA, Keniry MA, J Biol Chem. 2000 Apr 7;275(14):10009-15. PMID:10744677
Page seeded by OCA on Thu Jul 3 12:53:50 2008
