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1kla

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[[Image:1kla.gif|left|200px]]
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{{STRUCTURE_1kla| PDB=1kla | SCENE= }}
{{STRUCTURE_1kla| PDB=1kla | SCENE= }}
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'''SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 1-17 OF 33 STRUCTURES'''
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===SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 1-17 OF 33 STRUCTURES===
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==Overview==
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The three-dimensional solution structure of human transforming growth factor beta 1 (TGF-beta 1) has been determined using multinuclear magnetic resonance spectroscopy and a hybrid distance geometry/ simulated annealing algorithm. It represents one of the first examples of a mammalian protein structure that has been solved by isotopic labeling of the protein in a eukaryotic cell line and multinuclear NMR spectroscopy. The solution structure of the 25 kDa disulfide-linked TGF-beta 1 homodimer was calculated from over 3200 distance and dihedral angle restraints. The final ensemble of 33 accepted structures had no NOE or dihedral angle violations greater than 0.30 A and 5.0 degrees, respectively. The RMSD of backbone atoms for the ensemble of 33 structures relative to their mean structure was 1.1 A when all residues were used in the alignment and 0.7 A when loop regions were omitted. The solution structure of TGF-beta 1 follows two independently determined crystal structures of TGF-beta 2 (Daopin et al., 1992, 1993; Schlunegger &amp; Grutter, 1992, 1993), providing the first opportunity to examine structural differences between the two isoforms at the molecular level. Although the structures are very similar, with an RMSD in backbone atom positions of 1.4 A when loop regions are omitted in the alignment and 1.9 A when all residues are considered, there are several notable differences in structure and flexibility which may be related to function. The clearest example of these is in the beta-turn from residues 69-72: the turn type found in the solution structure of TGF-beta 1 falls into the category of type II, whereas that present in the X-ray crystal structure of TGF-beta 2 is more consistent with a type I turn conformation. This may be of functional significance as studies using TGF-beta chimeras and deletion mutants indicate that this portion of the molecule may be important in receptor binding.
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(as it appears on PubMed at http://www.pubmed.gov), where 8679613 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8679613}}
==About this Structure==
==About this Structure==
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1KLA 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=1KLA OCA].
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1KLA 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=1KLA OCA].
==Reference==
==Reference==
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[[Category: Growth factor]]
[[Category: Growth factor]]
[[Category: Mitogen]]
[[Category: Mitogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:52:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:30:15 2008''

Revision as of 07:30, 2 July 2008

Image:1kla.png

Template:STRUCTURE 1kla

SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 1-17 OF 33 STRUCTURES

Template:ABSTRACT PUBMED 8679613

About this Structure

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

Reference

Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2., Hinck AP, Archer SJ, Qian SW, Roberts AB, Sporn MB, Weatherbee JA, Tsang ML, Lucas R, Zhang BL, Wenker J, Torchia DA, Biochemistry. 1996 Jul 2;35(26):8517-34. PMID:8679613

Page seeded by OCA on Wed Jul 2 10:30:15 2008

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