1rj2

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(New page: 200px<br /><applet load="1rj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rj2, resolution 3.00&Aring;" /> '''Crystal structure of...)
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[[Image:1rj2.jpg|left|200px]]<br /><applet load="1rj2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rj2, resolution 3.00&Aring;" />
caption="1rj2, resolution 3.00&Aring;" />
'''Crystal structure of the DH/PH fragment of Dbs without bound GTPase'''<br />
'''Crystal structure of the DH/PH fragment of Dbs without bound GTPase'''<br />
==Overview==
==Overview==
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Dbl proteins are guanine nucleotide exchange factors for Rho GTPases, containing adjacent Dbl homology (DH) and pleckstrin homology (PH), domains. This domain architecture is virtually invariant and typically, required for full exchange potential. Several structures of DH/PH, fragments bound to GTPases implicate the PH domain in nucleotide exchange., To more fully understand the functional linkage between DH and PH domains, we have determined the crystal structure of the DH/PH fragment of Dbs, without bound GTPase. This structure is generally similar to previously, determined structures of Dbs bound to GTPases albeit with greater apparent, mobility between the DH and PH domains. These comparisons suggest that the, DH and PH domains of Dbs are spatially primed for binding GTPases and, small alterations in intradomain conformations that may be elicited by, subtle biological responses, such as altered phosphoinositide levels, are, sufficient to enhance exchange by facilitating interactions between the PH, domain and GTPases.
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Dbl proteins are guanine nucleotide exchange factors for Rho GTPases, containing adjacent Dbl homology (DH) and pleckstrin homology (PH) domains. This domain architecture is virtually invariant and typically required for full exchange potential. Several structures of DH/PH fragments bound to GTPases implicate the PH domain in nucleotide exchange. To more fully understand the functional linkage between DH and PH domains, we have determined the crystal structure of the DH/PH fragment of Dbs without bound GTPase. This structure is generally similar to previously determined structures of Dbs bound to GTPases albeit with greater apparent mobility between the DH and PH domains. These comparisons suggest that the DH and PH domains of Dbs are spatially primed for binding GTPases and small alterations in intradomain conformations that may be elicited by subtle biological responses, such as altered phosphoinositide levels, are sufficient to enhance exchange by facilitating interactions between the PH domain and GTPases.
==About this Structure==
==About this Structure==
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1RJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJ2 OCA].
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1RJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJ2 OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rossman, K.L.]]
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[[Category: Rossman, K L.]]
[[Category: Sondek, J.]]
[[Category: Sondek, J.]]
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[[Category: Worthylake, D.K.]]
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[[Category: Worthylake, D K.]]
[[Category: dbl homology; pleckstrin homology; guanine nucleotide exchange factor; rho gtpase]]
[[Category: dbl homology; pleckstrin homology; guanine nucleotide exchange factor; rho gtpase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:38:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:22 2008''

Revision as of 12:51, 21 February 2008


1rj2, resolution 3.00Å

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Crystal structure of the DH/PH fragment of Dbs without bound GTPase

Overview

Dbl proteins are guanine nucleotide exchange factors for Rho GTPases, containing adjacent Dbl homology (DH) and pleckstrin homology (PH) domains. This domain architecture is virtually invariant and typically required for full exchange potential. Several structures of DH/PH fragments bound to GTPases implicate the PH domain in nucleotide exchange. To more fully understand the functional linkage between DH and PH domains, we have determined the crystal structure of the DH/PH fragment of Dbs without bound GTPase. This structure is generally similar to previously determined structures of Dbs bound to GTPases albeit with greater apparent mobility between the DH and PH domains. These comparisons suggest that the DH and PH domains of Dbs are spatially primed for binding GTPases and small alterations in intradomain conformations that may be elicited by subtle biological responses, such as altered phosphoinositide levels, are sufficient to enhance exchange by facilitating interactions between the PH domain and GTPases.

About this Structure

1RJ2 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the DH/PH fragment of Dbs without bound GTPase., Worthylake DK, Rossman KL, Sondek J, Structure. 2004 Jun;12(6):1078-86. PMID:15274927

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