1e8a: Difference between revisions
New page: left|200px<br /> <applet load="1e8a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e8a, resolution 1.95Å" /> '''THE THREE-DIMENSION... |
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'''THE THREE-DIMENSIONAL STRUCTURE OF HUMAN S100A12'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF HUMAN S100A12'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1E8A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1E8A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8A OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:41:53 2008'' | ||
Revision as of 16:41, 15 February 2008
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THE THREE-DIMENSIONAL STRUCTURE OF HUMAN S100A12
OverviewOverview
The crystal structure of human EF-hand calcium-binding protein S100A12 in, its calcium-bound form has been determined to 1.95 A resolution by, molecular replacement using the structure of the S100B protein. The S100, family members are homologous to calmodulin and other related EF-hand, calcium-binding proteins. Like the majority of S100 proteins, S100A12 is a, dimer, with the interface between the two subunits being composed mostly, of hydrophobic residues. The fold of S100A12 is similar to the other known, crystal and solution structures of S100 proteins, except for the linker, region between the two EF-hand motifs. Sequence and structure comparison, between members of the S100 family suggests that the target-binding region, in S100A12 is formed by the linker region and C-terminal residues of one, subunit and the N-terminal residues of another subunit of the dimer. The, N-terminal region of the target-binding site includes two glutamates that, are conserved in most of the S100 sequences. The comparison also provided, a better understanding of the role of the residues important for intra-, and inter-subunit hydrophobic interactions. The precise role of S100A12 in, cell behaviour is yet undefined, as is the case for the whole family, although it has been shown that the interaction of S100A12 with the RAGE, receptor is implicated in inflammatory response.
About this StructureAbout this Structure
1E8A is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of human S100A12., Moroz OV, Antson AA, Murshudov GN, Maitland NJ, Dodson GG, Wilson KS, Skibshoj I, Lukanidin EM, Bronstein IB, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):20-9. PMID:11134923
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