1hi7
From Proteopedia
(New page: 200px<br /> <applet load="1hi7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hi7" /> '''NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LI...) |
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'''NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES'''<br /> | '''NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The trefoil factor family protein, TFF1, forms a homodimer, via a | + | The trefoil factor family protein, TFF1, forms a homodimer, via a disulphide linkage, that has greater activity in wound healing assays than the monomer. Having previously determined a high-resolution solution structure of a monomeric analogue of TFF1, we now investigate the structure of the homodimer formed by the native sequence. The two putative receptor/ligand recognition domains are found to be well separated, at opposite ends of a flexible linker. This contrasts sharply with the known fixed and compact arrangement of the two trefoil domains of the closely related TFF2, and has significant implications for the mechanism of action and functional specificity of the TFF of proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1HI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1HI7 is a [http://en.wikipedia.org/wiki/Single_protein 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=1HI7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Feeney, J.]] | [[Category: Feeney, J.]] | ||
| - | [[Category: Williams, M | + | [[Category: Williams, M A.]] |
[[Category: cell motility]] | [[Category: cell motility]] | ||
[[Category: growth factor]] | [[Category: growth factor]] | ||
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[[Category: tumor suppressor]] | [[Category: tumor suppressor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:28 2008'' |
Revision as of 11:01, 21 February 2008
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NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES
Overview
The trefoil factor family protein, TFF1, forms a homodimer, via a disulphide linkage, that has greater activity in wound healing assays than the monomer. Having previously determined a high-resolution solution structure of a monomeric analogue of TFF1, we now investigate the structure of the homodimer formed by the native sequence. The two putative receptor/ligand recognition domains are found to be well separated, at opposite ends of a flexible linker. This contrasts sharply with the known fixed and compact arrangement of the two trefoil domains of the closely related TFF2, and has significant implications for the mechanism of action and functional specificity of the TFF of proteins.
About this Structure
1HI7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1., Williams MA, Westley BR, May FE, Feeney J, FEBS Lett. 2001 Mar 30;493(2-3):70-4. PMID:11286998
Page seeded by OCA on Thu Feb 21 13:01:28 2008
