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[[Image:1igl.gif|left|200px]]
{{Seed}}
[[Image:1igl.png|left|200px]]


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{{STRUCTURE_1igl|  PDB=1igl  |  SCENE=  }}  
{{STRUCTURE_1igl|  PDB=1igl  |  SCENE=  }}  


'''SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIONSHIP TO RECEPTOR AND BINDING PROTEIN INTERACTIONS'''
===SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIONSHIP TO RECEPTOR AND BINDING PROTEIN INTERACTIONS===




==Overview==
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The three-dimensional structure of human insulin-like growth factor (IGF) II in aqueous solution at pH 3.1 and 300 K has been determined from nuclear magnetic resonance data and restrained molecular dynamics calculations. Structural constraints consisting of 502 NOE-derived distance constraints, 11 dihedral angle restraints, and three disulfide bridges were used as input for distance geometry calculations in DIANA and X-PLOR, followed by simulated annealing refinement and energy minimization in X-PLOR. The resulting family of 20 structures was well defined in the regions of residues 5 to 28 and 41 to 62, with an average pairwise root-mean-square deviation of 1.24 A for the backbone heavy-atoms (N, C2, C) and 1.90 A for all heavy atoms. The poorly defined regions consist of the N and C termini, part of the B-domain, and the C-domain loop. Resonances from these regions of the protein gave stronger cross peaks in two dimensional NMR spectra, consistent with significant motional averaging. The main secondary structure elements in IGF-II are alpha-helices encompassing residues 11 to 21, 42 to 49 and 53 to 59. A small anti-parallel beta-sheet is formed by residues 59 to 61 and 25 to 27, while residues 26 to 28 appear to participate in intermolecular beta-sheet formation. The structure of IGF-II in the well-defined regions is very similar to those of the corresponding regions of insulin and IGF-I. Significant differences between IGF-II and IGF-I occur near the start of the third helix, in a region known to modulate affinity for the type 2 IGF receptor, and at the C terminus. The IGF II structure is discussed in relation to its binding sites for the insulin and IGF receptors and the IGF binding proteins.
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{{ABSTRACT_PUBMED_7739048}}


==About this Structure==
==About this Structure==
1IGL 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=1IGL OCA].  
1IGL 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=1IGL OCA].  


==Reference==
==Reference==
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[[Category: Wallace, J C.]]
[[Category: Wallace, J C.]]
[[Category: Growth factor]]
[[Category: Growth factor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:58:30 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:28:33 2008''

Revision as of 17:28, 27 July 2008

File:1igl.png

Template:STRUCTURE 1igl

SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIONSHIP TO RECEPTOR AND BINDING PROTEIN INTERACTIONS

Template:ABSTRACT PUBMED 7739048

About this Structure

1IGL is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions., Torres AM, Forbes BE, Aplin SE, Wallace JC, Francis GL, Norton RS, J Mol Biol. 1995 Apr 28;248(2):385-401. PMID:7739048

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