2bwk: Difference between revisions

Revision as of 12:23, 28 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:2bwk.png

Template:STRUCTURE 2bwk

MURINE ANGIOGENIN, SULPHATE COMPLEXMURINE ANGIOGENIN, SULPHATE COMPLEX

Template:ABSTRACT PUBMED 16301790

About this StructureAbout this Structure

2BWK is a Single protein structure of sequence from Mus musculus. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2bwk|  PDB=2bwk  |  SCENE=  }}
-'''MURINE ANGIOGENIN, SULPHATE COMPLEX'''
+===MURINE ANGIOGENIN, SULPHATE COMPLEX===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16301790}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16301790}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Ribonuclease,angiogenesis,cancer]]
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