2qt4: Difference between revisions

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[[Image:2qt4.jpg|left|200px]]
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[[Image:2qt4.png|left|200px]]


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{{STRUCTURE_2qt4|  PDB=2qt4  |  SCENE=  }}  
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'''Atomic-resolution crystal structure of the natural form of Scytovirin'''
===Atomic-resolution crystal structure of the natural form of Scytovirin===




==Overview==
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The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single-wavelength anomalous scattering and refined with data extending to 1.3 A and 1.0 A resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 A for 40 pairs of Calpha atoms). The crystal structure differs significantly from a previously published NMR structure of the same protein, with the RMS deviations calculated separately for the N- and C-terminal domains of 5.3 A and 3.7 A, respectively, and a very different relationship between the two domains. In addition, the disulfide bonding pattern of the crystal structures differs from that described in the previously published mass spectrometry and NMR studies.
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{{ABSTRACT_PUBMED_17965185}}


==About this Structure==
==About this Structure==
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[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:38:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:52:51 2008''

Revision as of 09:52, 29 July 2008

File:2qt4.png

Template:STRUCTURE 2qt4

Atomic-resolution crystal structure of the natural form of Scytovirin

Template:ABSTRACT PUBMED 17965185

About this Structure

Full crystallographic information is available from OCA.

Reference

Atomic-resolution crystal structure of the antiviral lectin scytovirin., Moulaei T, Botos I, Ziolkowska NE, Bokesch HR, Krumpe LR, McKee TC, O'Keefe BR, Dauter Z, Wlodawer A, Protein Sci. 2007 Dec;16(12):2756-60. Epub 2007 Oct 26. PMID:17965185

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