1d2l: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1d2l.gif|left|200px]]<br /><applet load="1d2l" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1d2l.gif|left|200px]]
caption="1d2l" />
 
'''NMR SOLUTION STRUCTURE OF COMPLEMENT-LIKE REPEAT CR3 FROM THE LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN (LRP). EVIDENCE FOR SPECIFIC BINDING TO THE RECEPTOR BINDING DOMAIN OF HUMAN ALPHA-2 MACROGLOBULIN'''<br />
{{Structure
|PDB= 1d2l |SIZE=350|CAPTION= <scene name='initialview01'>1d2l</scene>
|SITE=  
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY=
|GENE=
}}
 
'''NMR SOLUTION STRUCTURE OF COMPLEMENT-LIKE REPEAT CR3 FROM THE LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN (LRP). EVIDENCE FOR SPECIFIC BINDING TO THE RECEPTOR BINDING DOMAIN OF HUMAN ALPHA-2 MACROGLOBULIN'''
 


==Overview==
==Overview==
Line 10: Line 19:


==About this Structure==
==About this Structure==
1D2L 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=1D2L OCA].  
1D2L 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=1D2L OCA].  


==Reference==
==Reference==
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin., Dolmer K, Huang W, Gettins PG, J Biol Chem. 2000 Feb 4;275(5):3264-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10652313 10652313]
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin., Dolmer K, Huang W, Gettins PG, J Biol Chem. 2000 Feb 4;275(5):3264-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10652313 10652313]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 25: Line 34:
[[Category: receptor]]
[[Category: receptor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:19 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:32:00 2008''

Revision as of 11:32, 20 March 2008

File:1d2l.gif


PDB ID 1d2l

Drag the structure with the mouse to rotate
Ligands:
Coordinates: save as pdb, mmCIF, xml



NMR SOLUTION STRUCTURE OF COMPLEMENT-LIKE REPEAT CR3 FROM THE LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN (LRP). EVIDENCE FOR SPECIFIC BINDING TO THE RECEPTOR BINDING DOMAIN OF HUMAN ALPHA-2 MACROGLOBULIN


OverviewOverview

We have used NMR methods to determine the structure of the calcium complex of complement-like repeat 3 (CR3) from the low density lipoprotein receptor-related protein (LRP) and to examine its specific interaction with the receptor binding domain of human alpha(2)-macroglobulin. CR3 is one of eight related repeats that constitute a major ligand binding region of LRP. The structure is very similar in overall fold to homologous complement-like repeat CR8 from LRP and complement-like repeats LB1, LB2, and LB5 from the low density lipoprotein receptor and contains a short two-strand antiparallel beta-sheet, a one turn alpha-helix, and a high affinity calcium site with coordination from four carboxyls and two backbone carbonyls. The surface electrostatics and topography are, however, quite distinct from each of these other repeats. Two-dimensional (1)H,(15)N-heteronuclear single quantum coherence spectra provide evidence for a specific, though relatively weak (K(d) approximately 140 microM), interaction between CR3 and human alpha2-macroglobulin receptor binding domain that involves a contiguous patch of surface residues in the central region of CR3. This specific interaction is consistent with a mode of LRP binding to ligands that uses contributions from more than one domain to generate a wide array of different binding sites, each with overall high affinity.

DiseaseDisease

Known diseases associated with this structure: Leigh syndrome, French-Canadian type OMIM:[607544], Urolithiasis, 2,8-dihydroxyadenine OMIM:[102600]

About this StructureAbout this Structure

1D2L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin., Dolmer K, Huang W, Gettins PG, J Biol Chem. 2000 Feb 4;275(5):3264-9. PMID:10652313

Page seeded by OCA on Thu Mar 20 10:32:00 2008

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

OCA