1p63

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[[Image:1p63.gif|left|200px]]
[[Image:1p63.gif|left|200px]]
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{{Structure
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|PDB= 1p63 |SIZE=350|CAPTION= <scene name='initialview01'>1p63</scene>, resolution 1.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1p63", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= FGF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1p63| PDB=1p63 | SCENE= }}
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|RELATEDENTRY=[[1jqz|1JQZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p63 OCA], [http://www.ebi.ac.uk/pdbsum/1p63 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p63 RCSB]</span>
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'''Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)'''
'''Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)'''
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[[Category: Kim, J.]]
[[Category: Kim, J.]]
[[Category: Logan, T M.]]
[[Category: Logan, T M.]]
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[[Category: beta-trefoil]]
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[[Category: Beta-trefoil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:43:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:55:21 2008''
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Revision as of 01:43, 3 May 2008

Template:STRUCTURE 1p63

Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)


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.

About this Structure

1P63 is a Single protein structure of sequence from Homo sapiens. 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 Sat May 3 04:43:51 2008

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