1ljy
From Proteopedia
(New page: 200px<br /><applet load="1ljy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ljy, resolution 2.90Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ljy.jpg|left|200px]]<br /><applet load="1ljy" size=" | + | [[Image:1ljy.jpg|left|200px]]<br /><applet load="1ljy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ljy, resolution 2.90Å" /> | caption="1ljy, resolution 2.90Å" /> | ||
'''Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution'''<br /> | '''Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the crystal structure of a novel regulatory protein | + | We have determined the crystal structure of a novel regulatory protein (MGP-40) from the mammary gland. This protein is implicated as a protective signaling factor that determines which cells are to survive the drastic tissue remodeling that occurs during involution. It has been indicated that certain cancers could surreptitiously utilize the proposed normal protective signaling by proteins of this family to extend their own survival and thereby allow them to invade the organ and metastasize. In view of this, MGP-40 could form an important target for rational structure-based drug design against breast cancer. It is a single chain, glycosylated protein with a molecular mass of 40 kDa. It was isolated from goat dry secretions and has been cloned and sequenced. It was crystallized by microdialysis from 20 mg ml(-1) solution in 0.1 m Tris-HCl, pH 8.0, and equilibrated against the same solution containing 19% ethanol. Its x-ray structure has been determined by molecular replacement and refined to a 2.9 A resolution. The protein adopts a beta/alpha domain structure with a triose-phosphate isomerase barrel conformation in the core and a small alpha+beta folding domain. A single glycosylation site containing two N-acetylglucosamine units has been observed in the structure. Compared with chitinases and chitinase-like proteins the most important mutation in this protein pertains to a change from Glu to Leu at position 119, which is part of the so-called active site sequence in the form of Asp(115), Leu(119), and Asp(186) and in this case resulting in the loss of chitinase activity. The orientations of two Trp residues Trp(78) and Trp(331) in the beta barrel reduces the free space, drastically impairing the binding of saccharides/polysaccharides. However, the site and mode of binding of this protein to cell surface receptors are not yet known. |
==About this Structure== | ==About this Structure== | ||
| - | 1LJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Capra_hircus Capra hircus] with NAG and NDG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Capra_hircus Capra hircus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kaur, P.]] | [[Category: Kaur, P.]] | ||
[[Category: Kumar, P.]] | [[Category: Kumar, P.]] | ||
| - | [[Category: Mohanty, A | + | [[Category: Mohanty, A K.]] |
[[Category: Paramasivam, M.]] | [[Category: Paramasivam, M.]] | ||
[[Category: Saravanan, K.]] | [[Category: Saravanan, K.]] | ||
[[Category: Sharma, S.]] | [[Category: Sharma, S.]] | ||
[[Category: Singh, G.]] | [[Category: Singh, G.]] | ||
| - | [[Category: Singh, T | + | [[Category: Singh, T P.]] |
[[Category: Srinivasan, A.]] | [[Category: Srinivasan, A.]] | ||
[[Category: Yadav, S.]] | [[Category: Yadav, S.]] | ||
| Line 31: | Line 31: | ||
[[Category: marker protein]] | [[Category: marker protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:37 2008'' |
Revision as of 11:45, 21 February 2008
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Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution
Overview
We have determined the crystal structure of a novel regulatory protein (MGP-40) from the mammary gland. This protein is implicated as a protective signaling factor that determines which cells are to survive the drastic tissue remodeling that occurs during involution. It has been indicated that certain cancers could surreptitiously utilize the proposed normal protective signaling by proteins of this family to extend their own survival and thereby allow them to invade the organ and metastasize. In view of this, MGP-40 could form an important target for rational structure-based drug design against breast cancer. It is a single chain, glycosylated protein with a molecular mass of 40 kDa. It was isolated from goat dry secretions and has been cloned and sequenced. It was crystallized by microdialysis from 20 mg ml(-1) solution in 0.1 m Tris-HCl, pH 8.0, and equilibrated against the same solution containing 19% ethanol. Its x-ray structure has been determined by molecular replacement and refined to a 2.9 A resolution. The protein adopts a beta/alpha domain structure with a triose-phosphate isomerase barrel conformation in the core and a small alpha+beta folding domain. A single glycosylation site containing two N-acetylglucosamine units has been observed in the structure. Compared with chitinases and chitinase-like proteins the most important mutation in this protein pertains to a change from Glu to Leu at position 119, which is part of the so-called active site sequence in the form of Asp(115), Leu(119), and Asp(186) and in this case resulting in the loss of chitinase activity. The orientations of two Trp residues Trp(78) and Trp(331) in the beta barrel reduces the free space, drastically impairing the binding of saccharides/polysaccharides. However, the site and mode of binding of this protein to cell surface receptors are not yet known.
About this Structure
1LJY is a Single protein structure of sequence from Capra hircus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution., Mohanty AK, Singh G, Paramasivam M, Saravanan K, Jabeen T, Sharma S, Yadav S, Kaur P, Kumar P, Srinivasan A, Singh TP, J Biol Chem. 2003 Apr 18;278(16):14451-60. Epub 2003 Jan 14. PMID:12529329
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