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| {{STRUCTURE_1jcd| PDB=1jcd | SCENE= }} | | {{STRUCTURE_1jcd| PDB=1jcd | SCENE= }} |
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| '''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=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12368282}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12368282 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12368282}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lipoprotein]] | | [[Category: Lipoprotein]] |
| [[Category: Protein folding]] | | [[Category: Protein folding]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:02:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:01:10 2008'' |