2f5h: Difference between revisions

Revision as of 17:28, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2f5h.png

Template:STRUCTURE 2f5h

Solution structure of the alpha-domain of human Metallothionein-3Solution structure of the alpha-domain of human Metallothionein-3

Template:ABSTRACT PUBMED 16413543

About this StructureAbout this Structure

2F5H is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Solution structure and dynamics of human metallothionein-3 (MT-3)., Wang H, Zhang Q, Cai B, Li H, Sze KH, Huang ZX, Wu HM, Sun H, FEBS Lett. 2006 Feb 6;580(3):795-800. Epub 2006 Jan 9. PMID:16413543

Page seeded by OCA on Sun Jul 27 17:28:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2f5h.gif|left|200px]]
+{{Seed}}
+[[Image:2f5h.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2f5h|  PDB=2f5h  |  SCENE=  }}
-'''Solution structure of the alpha-domain of human Metallothionein-3'''
+===Solution structure of the alpha-domain of human Metallothionein-3===
-==Overview==
+<!--
-Alzheimer's disease is characterized by progressive loss of neurons accompanied by the formation of intraneural neurofibrillary tangles and extracellular amyloid plaques. Human neuronal growth inhibitory factor, classified as metallothionein-3 (MT-3), was found to be related to the neurotrophic activity promoting cortical neuron survival and dendrite outgrowth in the cell culture studies. We have determined the solution structure of the alpha-domain of human MT-3 (residues 32-68) by multinuclear and multidimensional NMR spectroscopy in combination with the molecular dynamic simulated annealing approach. The human MT-3 shows two metal-thiolate clusters, one in the N-terminus (beta-domain) and one in the C-terminus (alpha-domain). The overall fold of the alpha-domain is similar to that of mouse MT-3. However, human MT-3 has a longer loop in the acidic hexapeptide insertion than that of mouse MT-3. Surprisingly, the backbone dynamics of the protein revealed that the beta-domain exhibits similar internal motion to the alpha-domain, although the N-terminal residues are more flexible. Our results may provide useful information for understanding the structure-function relationship of human MT-3.
+The line below this paragraph, {{ABSTRACT_PUBMED_16413543}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16413543 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16413543}}
 ==About this Structure==
-F5H 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=2F5H OCA].
+F5H 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=2F5H OCA].
 ==Reference==
@@ Line 32: / Line 36: @@
 [[Category: Alpha helix]]
 [[Category: Cadmium-thiolate cluster]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:29:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:28:08 2008''