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1p0t

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(New page: 200px<br /> <applet load="1p0t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p0t, resolution 3.30&Aring;" /> '''Crystal Structure o...)
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'''Crystal Structure of the BAFF-BAFF-R complex (part II)'''<br />
'''Crystal Structure of the BAFF-BAFF-R complex (part II)'''<br />
==Overview==
==Overview==
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B-cell activating factor (BAFF) is a key regulator of B-lymphocyte, development. Its biological role is mediated by the specific receptors, BCMA, TACI and BAFF-R. We have determined the crystal structure of the, extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 A. The, cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a, beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1, molar ratio. The conserved DxL motif of BAFF-R is located on the tip of, the beta-turn and is indispensable in the binding of BAFF. The crystal, structure shows that a unique dimeric contact occurs between the BAFF-R, monomers in the virus-like cage complex. The extracellular domain of TACI, contains two CRDs, both of which contain the DxL motif. Modeling of, TACI-BAFF complex suggests that both CDRs simultaneously interact with the, BAFF dimer in the virus-like cage.
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B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACI and BAFF-R. We have determined the crystal structure of the extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 A. The cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the beta-turn and is indispensable in the binding of BAFF. The crystal structure shows that a unique dimeric contact occurs between the BAFF-R monomers in the virus-like cage complex. The extracellular domain of TACI contains two CRDs, both of which contain the DxL motif. Modeling of TACI-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage.
==About this Structure==
==About this Structure==
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1P0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P0T OCA].
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1P0T is a [http://en.wikipedia.org/wiki/Single_protein 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=1P0T OCA].
==Reference==
==Reference==
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[[Category: stall]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:39:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:50 2008''

Revision as of 12:23, 21 February 2008

Image:1p0t.gif

1p0t, resolution 3.30Å

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Crystal Structure of the BAFF-BAFF-R complex (part II)

Overview

B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACI and BAFF-R. We have determined the crystal structure of the extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 A. The cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the beta-turn and is indispensable in the binding of BAFF. The crystal structure shows that a unique dimeric contact occurs between the BAFF-R monomers in the virus-like cage complex. The extracellular domain of TACI contains two CRDs, both of which contain the DxL motif. Modeling of TACI-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage.

About this Structure

1P0T is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation., Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO, Nat Struct Biol. 2003 May;10(5):342-8. PMID:12715002

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