1p0t

From Proteopedia

Revision as of 16:32, 12 November 2007

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

Page seeded by OCA on Mon Nov 12 18:39:16 2007