2hr9

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Solution structure of human translationally controlled tumor proteinSolution structure of human translationally controlled tumor protein

Structural highlights

2hr9 is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1y41. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TCTP_HUMAN Involved in calcium binding and microtubule stabilization.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human translationally controlled tumor protein (TCTP) is a growth-related, calcium-binding protein. We determined the solution structure and backbone dynamics of human TCTP, and identified the calcium-binding site of human TCTP using multi-dimensional NMR spectroscopy. The overall structure of human TCTP has a rather rigid well-folded core and a very flexible long loop connected by a short two-strand beta-sheet, which shows a conserved fold in the TCTP family. The C-terminal portions of loop L(alpha3beta8) and strand beta9 and the N-terminal region of strand beta8 may form a calcium-binding site in the human TCTP structure, which is largely conserved in the sequence alignment of TCTPs. The K(d) value for the calcium binding is 0.022-0.025 M indicating a very weak calcium-binding site.

Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR.,Feng Y, Liu D, Yao H, Wang J Arch Biochem Biophys. 2007 Nov 1;467(1):48-57. Epub 2007 Aug 30. PMID:17897616[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Feng Y, Liu D, Yao H, Wang J. Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR. Arch Biochem Biophys. 2007 Nov 1;467(1):48-57. Epub 2007 Aug 30. PMID:17897616 doi:10.1016/j.abb.2007.08.021
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