1rjh
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1rjh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rjh" /> '''Structure of the Calcium Free Form of the C...)
Next diff →
Revision as of 16:58, 12 November 2007
|
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
Page seeded by OCA on Mon Nov 12 19:04:31 2007
