3lri
From Proteopedia
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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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[[Category: Laajoki, L G.]] | [[Category: Laajoki, L G.]] | ||
[[Category: Wallace, J C.]] | [[Category: Wallace, J C.]] | ||
| - | [[Category: | + | [[Category: Distance geometry]] |
| - | [[Category: | + | [[Category: Growth factor]] |
| - | [[Category: | + | [[Category: Insulin-like growth factor-1]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 19:06, 4 May 2008
SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF HUMAN LONG-[ARG3]INSULIN-LIKE GROWTH FACTOR 1
Overview
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.
About this Structure
3LRI is a Single protein structure of sequence from Homo sapiens. Full crystallographic 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 Sun May 4 22:06:04 2008
