2akf
From Proteopedia
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| - | [[Image:2akf.gif|left|200px]] | + | [[Image:2akf.gif|left|200px]] |
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| - | '''Crystal structure of the coiled-coil domain of coronin 1''' | + | {{Structure |
| + | |PDB= 2akf |SIZE=350|CAPTION= <scene name='initialview01'>2akf</scene>, resolution 1.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the coiled-coil domain of coronin 1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AKF is a [ | + | 2AKF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKF OCA]. |
==Reference== | ==Reference== | ||
| - | A conserved trimerization motif controls the topology of short coiled coils., Kammerer RA, Kostrewa D, Progias P, Honnappa S, Avila D, Lustig A, Winkler FK, Pieters J, Steinmetz MO, Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13891-6. Epub 2005 Sep 19. PMID:[http:// | + | A conserved trimerization motif controls the topology of short coiled coils., Kammerer RA, Kostrewa D, Progias P, Honnappa S, Avila D, Lustig A, Winkler FK, Pieters J, Steinmetz MO, Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13891-6. Epub 2005 Sep 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16172398 16172398] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Avila, D.]] | [[Category: Avila, D.]] | ||
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[[Category: coronin 1]] | [[Category: coronin 1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:50:43 2008'' |
Revision as of 13:50, 20 March 2008
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| , resolution 1.20Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the coiled-coil domain of coronin 1
Overview
In recent years, short coiled coils have been used for applications ranging from biomaterial to medical sciences. For many of these applications knowledge of the factors that control the topology of the engineered protein systems is essential. Here, we demonstrate that trimerization of short coiled coils is determined by a distinct structural motif that encompasses specific networks of surface salt bridges and optimal hydrophobic packing interactions. The motif is conserved among intracellular, extracellular, viral, and synthetic proteins and defines a universal molecular determinant for trimer formation of short coiled coils. In addition to being of particular interest for the biotechnological production of candidate therapeutic proteins, these findings may be of interest for viral drug development strategies.
About this Structure
2AKF is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
A conserved trimerization motif controls the topology of short coiled coils., Kammerer RA, Kostrewa D, Progias P, Honnappa S, Avila D, Lustig A, Winkler FK, Pieters J, Steinmetz MO, Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13891-6. Epub 2005 Sep 19. PMID:16172398
Page seeded by OCA on Thu Mar 20 15:50:43 2008
