3baq: Difference between revisions

Revision as of 09:24, 28 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:3baq.png

Template:STRUCTURE 3baq

Crystal structure of L26A mutant of Human acidic fibroblast growth factorCrystal structure of L26A mutant of Human acidic fibroblast growth factor

Template:ABSTRACT PUBMED 18308335

About this StructureAbout this Structure

3BAQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif., Lee J, Dubey VK, Longo LM, Blaber M, J Mol Biol. 2008 Apr 4;377(4):1251-64. Epub 2008 Jan 31. PMID:18308335

Page seeded by OCA on Mon Jul 28 09:24:05 2008

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

OCA

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-[[Image:3baq.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_3baq|  PDB=3baq  |  SCENE=  }}
-'''Crystal structure of L26A mutant of Human acidic fibroblast growth factor'''
+===Crystal structure of L26A mutant of Human acidic fibroblast growth factor===
-==Overview==
+<!--
-Turn secondary structure is essential to the formation of globular protein architecture. Turn structures are, however, much more complex than either alpha-helix or beta-sheet, and the thermodynamics and folding kinetics are poorly understood. Type I beta-turns are the most common type of reverse turn, and they exhibit a statistical consensus sequence of Asx-Pro-Asx-Gly (where Asx is Asp or Asn). A comprehensive series of individual and combined Asx mutations has been constructed within three separate type I 3:5 G1 bulge beta-turns in human fibroblast growth factor-1, and their effects on structure, stability, and folding have been determined. The results show a fundamental logical OR relationship between the Asx residues in the motif, involving H-bond interactions with main-chain amides within the turn. These interactions can be modulated by additional interactions with residues adjacent to the turn at positions i+4 and i+6. The results show that the Asx residues in the turn motif make a substantial contribution to the overall stability of the protein, and the Asx logical OR relationship defines a redundant system that can compensate for deleterious point mutations. The results also show that the stability of the turn is unlikely to be the prime determinant of formation of turn structure in the folding transition state.
+The line below this paragraph, {{ABSTRACT_PUBMED_18308335}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18308335 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18308335}}
 ==About this Structure==
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 [[Category: Mitogen]]
 [[Category: Polymorphism]]
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