1mhq

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(New page: 200px<br /> <applet load="1mhq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mhq, resolution 2.2&Aring;" /> '''Crystal Structure Of...)
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<applet load="1mhq" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1mhq, resolution 2.2&Aring;" />
caption="1mhq, resolution 2.2&Aring;" />
'''Crystal Structure Of Human GGA2 VHS Domain'''<br />
'''Crystal Structure Of Human GGA2 VHS Domain'''<br />
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==About this Structure==
==About this Structure==
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1MHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MHQ OCA].
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1MHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHQ OCA].
==Reference==
==Reference==
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[[Category: super helix]]
[[Category: super helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:11:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:24:24 2008''

Revision as of 14:24, 15 February 2008


1mhq, resolution 2.2Å

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Crystal Structure Of Human GGA2 VHS Domain

Overview

Golgi-localized, gamma-ear-containing, ARF binding (GGA) proteins regulate, intracellular vesicle transport by recognizing sorting signals on the, cargo surface in the initial step of the budding process. The VHS (VPS27, Hrs, and STAM) domain of GGA binds with the signal peptides. Here, a, crystal structure of the VHS domain of GGA2 is reported at 2.2 A, resolution, which permits a direct comparison with that of homologous, proteins, GGA1 and GGA3. Significant structural difference is present in, the loop between helices 6 and 7, which forms part of the ligand binding, pocket. Intrinsic fluorescence spectroscopic study indicates that this, loop undergoes a conformational change upon ligand binding. Thus, the, current structure suggests that a conformational change induced by ligand, binding occurs in this part of the ligand pocket.

About this Structure

1MHQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket., Zhu G, He X, Zhai P, Terzyan S, Tang J, Zhang XC, FEBS Lett. 2003 Feb 27;537(1-3):171-6. PMID:12606052

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