1rjh
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Tetranectin is a homotrimeric protein containing a C-type lectin-like | + | Tetranectin is a homotrimeric protein containing a C-type lectin-like domain. This domain (TN3) can bind calcium, but in the absence of calcium, the domain binds a number of kringle-type protein ligands. Two of the calcium-coordinating residues are also critical for binding plasminogen kringle 4 (K4). The structure of the calcium free-form of TN3 (apoTN3) has been determined by NMR. Compared to the structure of the calcium-bound form of TN3 (holoTN3), the core region of secondary structural elements is conserved, while large displacements occur in the loops involved in calcium or K4 binding. A conserved proline, which was found to be in the cis conformation in holoTN3, is in apoTN3 predominantly in the trans conformation. Backbone dynamics indicate that, in apoTN3 especially, two of the three calcium-binding loops and two of the three K4-binding residues exhibit increased flexibility, whereas no such flexibility is observed in holoTN3. In the 20 best nuclear magnetic resonance structures of apoTN3, the residues critical for K4 binding span a large conformational space. Together with the relaxation data, this indicates that the K4-ligand-binding site in apoTN3 is not preformed. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Etzerodt, M.]] | [[Category: Etzerodt, M.]] | ||
| - | [[Category: Graversen, J | + | [[Category: Graversen, J H.]] |
[[Category: Nielbo, S.]] | [[Category: Nielbo, S.]] | ||
| - | [[Category: Poulsen, F | + | [[Category: Poulsen, F M.]] |
| - | [[Category: Thoegersen, H | + | [[Category: Thoegersen, H C.]] |
| - | [[Category: Thomsen, J | + | [[Category: Thomsen, J K.]] |
[[Category: apo]] | [[Category: apo]] | ||
[[Category: c-type lectin-like domain]] | [[Category: c-type lectin-like domain]] | ||
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[[Category: trans proline]] | [[Category: trans proline]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:30 2008'' |
Revision as of 12:51, 21 February 2008
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Structure of the Calcium Free Form of the C-type Lectin-like Domain of Tetranectin
Overview
Tetranectin is a homotrimeric protein containing a C-type lectin-like domain. This domain (TN3) can bind calcium, but in the absence of calcium, the domain binds a number of kringle-type protein ligands. Two of the calcium-coordinating residues are also critical for binding plasminogen kringle 4 (K4). The structure of the calcium free-form of TN3 (apoTN3) has been determined by NMR. Compared to the structure of the calcium-bound form of TN3 (holoTN3), the core region of secondary structural elements is conserved, while large displacements occur in the loops involved in calcium or K4 binding. A conserved proline, which was found to be in the cis conformation in holoTN3, is in apoTN3 predominantly in the trans conformation. Backbone dynamics indicate that, in apoTN3 especially, two of the three calcium-binding loops and two of the three K4-binding residues exhibit increased flexibility, whereas no such flexibility is observed in holoTN3. In the 20 best nuclear magnetic resonance structures of apoTN3, the residues critical for K4 binding span a large conformational space. Together with the relaxation data, this indicates that the K4-ligand-binding site in apoTN3 is not preformed.
About this Structure
1RJH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the plasminogen kringle 4 binding calcium-free form of the C-type lectin-like domain of tetranectin., Nielbo S, Thomsen JK, Graversen JH, Jensen PH, Etzerodt M, Poulsen FM, Thogersen HC, Biochemistry. 2004 Jul 13;43(27):8636-43. PMID:15236571
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