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| - | [[Image:1htj.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1htj| PDB=1htj | SCENE= }} | | {{STRUCTURE_1htj| PDB=1htj | SCENE= }} |
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| - | '''STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF'''
| + | ===STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF=== |
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| - | ==Overview==
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| - | BACKGROUND: The multidomain PDZ-RhoGEF is one of many known guanine nucleotide exchange factors that upregulate Rho GTPases. PDZ-RhoGEF and related family members play a critical role in a molecular signaling pathway from heterotrimeric G protein-coupled receptors to Rho proteins. A approximately 200 residue RGS-like (RGSL) domain in PDZ-RhoGEF and its homologs is responsible for the direct association with Galpha12/13 proteins. To better understand structure-function relationships, we initiated crystallographic studies of the RGSL domain from human PDZ-RhoGEF. RESULTS: A recombinant construct of the RGSL domain was expressed in Escherichia coli and purified, but it did not crystallize. Alternative constructs were designed based on a novel strategy of targeting lysine and glutamic acid residues for mutagenesis to alanine. A triple-point mutant functionally identical to the wild-type protein was crystallized, and its structure was determined by the MAD method using Se-methionine (Se-Met) incorporation. A molecular model of the RGSL domain was refined at 2.2 A resolution, revealing an all-helical tertiary fold with the mutations located at intermolecular lattice contacts. CONCLUSIONS: The first nine helices adopt a fold similar to that observed for RGS proteins, although the sequence identity with other such known structures is below 20%. The last three helices are an integral extension of the RGS fold, packing tightly against helices 3 and 4 with multiple hydrophobic interactions. Comparison with RGS proteins suggests features that are likely relevant for interaction with G proteins. Finally, we conclude that the strategy used to produce crystals was beneficial and might be applicable to other proteins resistant to crystallization.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11470431}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11470431 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11470431}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Regulator of g protein signaling]] | | [[Category: Regulator of g protein signaling]] |
| | [[Category: Rgs-like]] | | [[Category: Rgs-like]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:13:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:39:33 2008'' |
Revision as of 05:39, 1 July 2008
Template:STRUCTURE 1htj
STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF
Template:ABSTRACT PUBMED 11470431
About this Structure
1HTJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g protein-coupled signaling to Rho GTPases., Longenecker KL, Lewis ME, Chikumi H, Gutkind JS, Derewenda ZS, Structure. 2001 Jul 3;9(7):559-69. PMID:11470431
Page seeded by OCA on Tue Jul 1 08:39:33 2008
