1egg

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(New page: 200px<br /> <applet load="1egg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1egg, resolution 2.30&Aring;" /> '''STRUCTURE OF A C-TY...)
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'''STRUCTURE OF A C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD-4) FROM THE MACROPHAGE MANNOSE RECEPTOR'''<br />
'''STRUCTURE OF A C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD-4) FROM THE MACROPHAGE MANNOSE RECEPTOR'''<br />
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==About this Structure==
==About this Structure==
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1EGG 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EGG OCA].
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1EGG 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=1EGG OCA].
==Reference==
==Reference==
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[[Category: mannose receptor]]
[[Category: mannose receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:43:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:12 2008''

Revision as of 13:43, 15 February 2008


1egg, resolution 2.30Å

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STRUCTURE OF A C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD-4) FROM THE MACROPHAGE MANNOSE RECEPTOR

Overview

The mannose receptor of macrophages and liver endothelium mediates, clearance of pathogenic organisms and potentially harmful glycoconjugates., The extracellular portion of the receptor includes eight C-type, carbohydrate recognition domains (CRDs), of which one, CRD-4, shows, detectable binding to monosaccharide ligands. We have determined the, crystal structure of CRD-4. Although the basic C-type lectin fold is, preserved, a loop extends away from the core of the domain to form a, domain-swapped dimer in the crystal. Of the two Ca(2+) sites, only the, principal site known to mediate carbohydrate binding in other C-type, lectins is occupied. This site is altered in a way that makes sugar, binding impossible in the mode observed in other C-type lectins. The, structure is likely to represent an endosomal form of the domain formed, when Ca(2+) is lost from the auxiliary calcium site. The structure, suggests a mechanism for endosomal ligand release in which the auxiliary, calcium site serves as a pH sensor. Acid pH-induced removal of this Ca(2+), results in conformational rearrangements of the receptor, rendering it, unable to bind carbohydrate ligands.

About this Structure

1EGG is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor., Feinberg H, Park-Snyder S, Kolatkar AR, Heise CT, Taylor ME, Weis WI, J Biol Chem. 2000 Jul 14;275(28):21539-48. PMID:10779515

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