2akf

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(New page: 200px<br /><applet load="2akf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2akf, resolution 1.20&Aring;" /> '''Crystal structure of...)
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[[Image:2akf.gif|left|200px]]<br /><applet load="2akf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2akf.gif|left|200px]]<br /><applet load="2akf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2akf, resolution 1.20&Aring;" />
caption="2akf, resolution 1.20&Aring;" />
'''Crystal structure of the coiled-coil domain of coronin 1'''<br />
'''Crystal structure of the coiled-coil domain of coronin 1'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2AKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AKF OCA].
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2AKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKF OCA].
==Reference==
==Reference==
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[[Category: Avila, D.]]
[[Category: Avila, D.]]
[[Category: Honnappa, S.]]
[[Category: Honnappa, S.]]
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[[Category: Kammerer, R.A.]]
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[[Category: Kammerer, R A.]]
[[Category: Kostrewa, D.]]
[[Category: Kostrewa, D.]]
[[Category: Lustig, A.]]
[[Category: Lustig, A.]]
[[Category: Pieters, J.]]
[[Category: Pieters, J.]]
[[Category: Progias, P.]]
[[Category: Progias, P.]]
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[[Category: Steinmetz, M.O.]]
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[[Category: Steinmetz, M O.]]
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[[Category: Winkler, F.K.]]
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[[Category: Winkler, F K.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: coiled coil]]
[[Category: coiled coil]]
[[Category: coronin 1]]
[[Category: coronin 1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:11:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:17 2008''

Revision as of 14:28, 21 February 2008


2akf, resolution 1.20Å

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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] with as ligand. 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 Feb 21 16:28:17 2008

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