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3lri

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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'''
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===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) --&gt; 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.
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{{ABSTRACT_PUBMED_10744677}}
==About this Structure==
==About this Structure==
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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].
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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].
==Reference==
==Reference==
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[[Category: Nmr]]
[[Category: Nmr]]
[[Category: Protein structure]]
[[Category: Protein structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:06:04 2008''
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''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

Image:3lri.png

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

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