1tr4: Difference between revisions

Revision as of 08:13, 29 July 2008

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File:1tr4.png

Template:STRUCTURE 1tr4

Solution structure of human oncogenic protein gankyrinSolution structure of human oncogenic protein gankyrin

Template:ABSTRACT PUBMED 15379554

About this StructureAbout this Structure

1TR4 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Solution structure of the human oncogenic protein gankyrin containing seven ankyrin repeats and analysis of its structure--function relationship., Yuan C, Li J, Mahajan A, Poi MJ, Byeon IJ, Tsai MD, Biochemistry. 2004 Sep 28;43(38):12152-61. PMID:15379554

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 {{STRUCTURE_1tr4|  PDB=1tr4  |  SCENE=  }}
-'''Solution structure of human oncogenic protein gankyrin'''
+===Solution structure of human oncogenic protein gankyrin===
-==Overview==
+<!--
-Human gankyrin (226 residues, 24.4 kDa) is a liver oncoprotein that plays an important role in the development of human hepatocellular carcinomas. In this paper, its solution structure is reported, which is the largest ankyrin protein ever determined by NMR. The highly degenerate primary sequences of the seven ankyrin repeats presented a major challenge, which was overcome by combined use of TROSY experiments, perdeuterated samples, isotope-filtered NMR experiments, and residual dipolar couplings. The final structure was of high quality, with atomic rmsds for the backbone (N, C', and C(alpha)) and all heavy atoms (residues 4-224) of 0.69 +/- 0.09 and 1.04 +/- 0.09 A, respectively. Detailed analyses of NMR data suggested that the conserved TPLH motifs play important structural roles in stabilizing the repeating ankyrin scaffold. Gankyrin is conformationally more stable than the tumor suppressor p16(INK4A), possibly due to the structural roles of conserved residues evidenced by slowly exchanging backbone amides as well as hydrogen bonding networks involving labile side chain protons. Structural comparison with p16(INK4A) identified several residues of gankyrin that are potentially important for CDK4 binding, whereas observation of the thiol proton of C180 indicated a well-structured Rb-binding site in the helical region of the sixth ankyrin repeat. Interestingly, the CDK4-binding site and Rb-binding site located in N- and C-terminal regions, respectively, are separated by comparatively more stable ankyrin repeats and highly condensed positive surface charge. These results and analyses will shed light on the structural basis of the function of human gankyrin.
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+{{ABSTRACT_PUBMED_15379554}}
 ==About this Structure==
-TR4 is a [[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=1TR4 OCA].
+TR4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TR4 OCA].
 ==Reference==
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 [[Category: Oncoprotein]]
 [[Category: Protein structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:16:32 2008''
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