1iq3: Difference between revisions

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==Overview==

The solution structure of the Eps15 homology (EH) domain of a human POB1, (partner of RaIBP1) has been determined by uniform 13C/15N labeling and, heteronuclear multidimensional nuclear magnetic resonance spectroscopy., The POB1 EH domain consists of two EF-hand structures, and the second one, binds a calcium ion. In the calcium-bound state, the orientation of the, fourth alpha-helix relative to the other helices of the POB1 EH domain is, slightly different from that of calbindin, and much more different from, those of calmodulin and troponin C, on the basis of their atomic, coordinates.

The solution structure of the Eps15 homology (EH) domain of a human POB1 (partner of RaIBP1) has been determined by uniform 13C/15N labeling and heteronuclear multidimensional nuclear magnetic resonance spectroscopy. The POB1 EH domain consists of two EF-hand structures, and the second one binds a calcium ion. In the calcium-bound state, the orientation of the fourth alpha-helix relative to the other helices of the POB1 EH domain is slightly different from that of calbindin, and much more different from those of calmodulin and troponin C, on the basis of their atomic coordinates.

==About this Structure==

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[[Category: Kikuchi, A.]]

[[Category: Koshiba, S.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Yokoyama, S.]]

[[Category: CA]]

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[[Category: structural genomics]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:22 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The solution structure of the Eps15 homology (EH) domain of a human POB1, (partner of RaIBP1) has been determined by uniform 13C/15N labeling and, heteronuclear multidimensional nuclear magnetic resonance spectroscopy., The POB1 EH domain consists of two EF-hand structures, and the second one, binds a calcium ion. In the calcium-bound state, the orientation of the, fourth alpha-helix relative to the other helices of the POB1 EH domain is, slightly different from that of calbindin, and much more different from, those of calmodulin and troponin C, on the basis of their atomic, coordinates.
+The solution structure of the Eps15 homology (EH) domain of a human POB1 (partner of RaIBP1) has been determined by uniform 13C/15N labeling and heteronuclear multidimensional nuclear magnetic resonance spectroscopy. The POB1 EH domain consists of two EF-hand structures, and the second one binds a calcium ion. In the calcium-bound state, the orientation of the fourth alpha-helix relative to the other helices of the POB1 EH domain is slightly different from that of calbindin, and much more different from those of calmodulin and troponin C, on the basis of their atomic coordinates.
 ==About this Structure==
@@ Line 17: / Line 17: @@
 [[Category: Kikuchi, A.]]
 [[Category: Koshiba, S.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Yokoyama, S.]]
 [[Category: CA]]
@@ Line 26: / Line 26: @@
 [[Category: structural genomics]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:03:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:22 2008''