1jcd: Difference between revisions

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[[Image:1jcd.gif|left|200px]]
{{Seed}}
[[Image:1jcd.png|left|200px]]


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{{STRUCTURE_1jcd|  PDB=1jcd  |  SCENE=  }}  
{{STRUCTURE_1jcd|  PDB=1jcd  |  SCENE=  }}  


'''Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations'''
===Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations===




==Overview==
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A major challenge in protein folding is to identify and quantify specific structural determinants that allow native proteins to acquire their unique folded structures. Here we report the engineering of a 52-residue protein (Ala-14) that contains exclusively alanine residues at the hydrophobic a and d positions of a natural heptad-repeat sequence. Ala-14 is unfolded under normal solution conditions yet forms a parallel three-stranded alpha-helical coiled coil in crystals. Ala-14 trimers in the solid state associate with each other through the pairing of polar side chains and formation of an extended network of water-mediated hydrogen bonds. In contrast to the classical view that local intramolecular tertiary interactions dictate the three-dimensional structure of small single-domain proteins, Ala-14 shows that long range intermolecular interactions can be essential in determining the metastable alanine-zipper structure. A similar interplay between short range local and longer range global forces may underlie the conformational properties of the growing class of natively unstructured proteins in biological processes.
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{{ABSTRACT_PUBMED_12368282}}


==About this Structure==
==About this Structure==
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[[Category: Lipoprotein]]
[[Category: Lipoprotein]]
[[Category: Protein folding]]
[[Category: Protein folding]]
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