1fwo: Difference between revisions

Revision as of 04:03, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fwo.png

Template:STRUCTURE 1fwo

THE SOLUTION STRUCTURE OF A 35-RESIDUE FRAGMENT FROM THE GRANULIN/EPITHELIN-LIKE SUBDOMAIN OF RICE ORYZAIN BETA (ROB 382-416 (C398S,C399S,C407S,C413S))THE SOLUTION STRUCTURE OF A 35-RESIDUE FRAGMENT FROM THE GRANULIN/EPITHELIN-LIKE SUBDOMAIN OF RICE ORYZAIN BETA (ROB 382-416 (C398S,C399S,C407S,C413S))

Template:ABSTRACT PUBMED 11298924

About this StructureAbout this Structure

1FWO is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

A peptide derived from the C-terminal part of a plant cysteine protease folds into a stack of two beta-hairpins, a scaffold present in the emerging family of granulin-like growth factors., Tolkatchev D, Xu P, Ni F, J Pept Res. 2001 Mar;57(3):227-33. PMID:11298924

Page seeded by OCA on Tue Jul 1 04:03:29 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1fwo.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1fwo|  PDB=1fwo  |  SCENE=  }}
-'''THE SOLUTION STRUCTURE OF A 35-RESIDUE FRAGMENT FROM THE GRANULIN/EPITHELIN-LIKE SUBDOMAIN OF RICE ORYZAIN BETA (ROB 382-416 (C398S,C399S,C407S,C413S))'''
+===THE SOLUTION STRUCTURE OF A 35-RESIDUE FRAGMENT FROM THE GRANULIN/EPITHELIN-LIKE SUBDOMAIN OF RICE ORYZAIN BETA (ROB 382-416 (C398S,C399S,C407S,C413S))===
-==Overview==
+<!--
-A 35 amino acid residue peptide corresponding to the N-terminal subdomain of the granulin-like repeat from rice oryzain beta was synthesized and regioselectively oxidized to produce a species with a [1-3, 2-4] disulfide-pairing pattern. The resulting peptide was studied in solution using NMR and was shown to adopt the tertiary topology of a stack of two beta-hairpins found in the emerging family of granulin-like growth factors. Because of the longer second beta-hairpin, the overall conformation of the peptide is somewhat more flexible than that of its well-structured carp granulin-1 analog. Except for the cysteine alignment, there is very little sequence homology between granulin-like growth factors from the animal kingdom and the granulin-like repeats at the C-termini of plant cysteine proteases. Therefore, the stack of two beta-hairpins may be a conserved three-dimensional organization of the granulin-like repeats from evolutionary distant sources with a significant role in specific protein-protein interactions.
+The line below this paragraph, {{ABSTRACT_PUBMED_11298924}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11298924 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11298924}}
 ==About this Structure==
-FWO is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FWO OCA].
+FWO is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FWO OCA].
 ==Reference==
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 [[Category: Beta-hairpin stack fold]]
 [[Category: Granulin/epithelin-like protein repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:51:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:03:29 2008''