1m16
From Proteopedia
(New page: 200px<br /> <applet load="1m16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m16, resolution 1.70Å" /> '''Human Acidic Fibrob...) |
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| - | [[Image:1m16.gif|left|200px]]<br /> | + | [[Image:1m16.gif|left|200px]]<br /><applet load="1m16" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1m16" size=" | + | |
caption="1m16, resolution 1.70Å" /> | caption="1m16, resolution 1.70Å" /> | ||
'''Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).'''<br /> | '''Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).'''<br /> | ||
==Overview== | ==Overview== | ||
| - | An alternative core packing group, involving a set of five positions, has | + | An alternative core packing group, involving a set of five positions, has been introduced into human acidic FGF-1. This alternative group was designed so as to constrain the primary structure within the core region to the same threefold symmetry present in the tertiary structure of the protein fold (the beta-trefoil superfold). The alternative core is essentially indistinguishable from the WT core with regard to structure, stability, and folding kinetics. The results show that the beta-trefoil superfold is compatible with a threefold symmetric constraint on the core region, as might be the case if the superfold arose as a result of gene duplication/fusion events. Furthermore, this new core arrangement can form the basis of a structural "building block" that can greatly simplify the de novo design of beta-trefoil proteins by using symmetric structural complementarity. Remaining asymmetry within the core appears to be related to asymmetry in the tertiary structure associated with receptor and heparin binding functionality of the growth factor. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1M16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M16 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blaber, M.]] | [[Category: Blaber, M.]] | ||
| - | [[Category: Brych, S | + | [[Category: Brych, S R.]] |
[[Category: Kim, J.]] | [[Category: Kim, J.]] | ||
| - | [[Category: Logan, T | + | [[Category: Logan, T M.]] |
| - | [[Category: Spielmann, G | + | [[Category: Spielmann, G L.]] |
[[Category: FMT]] | [[Category: FMT]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: beta-trefoil]] | [[Category: beta-trefoil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:23 2008'' |
Revision as of 11:50, 21 February 2008
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Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).
Contents |
Overview
An alternative core packing group, involving a set of five positions, has been introduced into human acidic FGF-1. This alternative group was designed so as to constrain the primary structure within the core region to the same threefold symmetry present in the tertiary structure of the protein fold (the beta-trefoil superfold). The alternative core is essentially indistinguishable from the WT core with regard to structure, stability, and folding kinetics. The results show that the beta-trefoil superfold is compatible with a threefold symmetric constraint on the core region, as might be the case if the superfold arose as a result of gene duplication/fusion events. Furthermore, this new core arrangement can form the basis of a structural "building block" that can greatly simplify the de novo design of beta-trefoil proteins by using symmetric structural complementarity. Remaining asymmetry within the core appears to be related to asymmetry in the tertiary structure associated with receptor and heparin binding functionality of the growth factor.
Disease
Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]
About this Structure
1M16 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Accommodation of a highly symmetric core within a symmetric protein superfold., Brych SR, Kim J, Logan TM, Blaber M, Protein Sci. 2003 Dec;12(12):2704-18. PMID:14627732
Page seeded by OCA on Thu Feb 21 13:50:23 2008
Categories: Homo sapiens | Single protein | Blaber, M. | Brych, S R. | Kim, J. | Logan, T M. | Spielmann, G L. | FMT | SO4 | Beta-trefoil
