2bwk: Difference between revisions
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[[Image:2bwk.gif|left|200px]]<br /><applet load="2bwk" size=" | [[Image:2bwk.gif|left|200px]]<br /><applet load="2bwk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2bwk, resolution 1.50Å" /> | caption="2bwk, resolution 1.50Å" /> | ||
'''MURINE ANGIOGENIN, SULPHATE COMPLEX'''<br /> | '''MURINE ANGIOGENIN, SULPHATE COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2BWK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 2BWK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWK OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:28:36 2008'' | ||
Revision as of 11:28, 3 February 2008
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MURINE ANGIOGENIN, SULPHATE COMPLEX
OverviewOverview
Angiogenin is an unusual member of the pancreatic ribonuclease superfamily, that induces blood-vessel formation and is a promising anticancer target., The three-dimensional structure of murine angiogenin (mAng) has been, determined by X-ray crystallography. Two structures are presented: one is, a complex with sulfate ions (1.5 Angstroms resolution) and the other a, complex with phosphate ions (1.6 Angstroms resolution). Residues forming, the putative B(1), P(1) and B(2) subsites occupy positions similar to, their hAng counterparts and are likely to play similar roles. The anions, occupy the P(1) subsite, sulfate binding conventionally and phosphate, adopting two orientations, one of which is novel. The B(1) subsite is, obstructed by Glu116 and Phe119, with the latter assuming a less invasive, position than its hAng counterpart. Hydrophobic interactions between the, C-terminal segment and the main body of the protein are more extensive, than in hAng and may underly the lower enzymatic activity of the murine, protein. Elsewhere, the structure of the H3-B2 loop supports the view that, hAng Asn61 interacts directly with cell-surface molecules and does not, merely stabilize adjacent regions of the hAng structure. mAng crystals, appear to offer small-molecule inhibitors a clear route to the active site, and may even withstand a reorientation of the C-terminal segment that, provides access to the cryptic B(1) subsite. These features represent, considerable advantages over crystalline hAng and bAng.
About this StructureAbout this Structure
2BWK is a Single protein structure of sequence from Mus musculus with as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structure of murine angiogenin: features of the substrate- and cell-binding regions and prospects for inhibitor-binding studies., Holloway DE, Chavali GB, Hares MC, Subramanian V, Acharya KR, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1568-78. Epub 2005, Nov 19. PMID:16301790
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